Exam 1 Flashcards

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1
Q

All biological systems are composed of

A

cells containing the same types of chemical molecules and employing similar principles of organization at the cellular level

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2
Q

All living organisms descended from a common

A

ancestral cell

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3
Q

___ and ___ gave rise to new organisms during evolution

A

gene duplications; mutations

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4
Q

Tree branch relationships were assigned by similarities in

A

organismal morphological features and in DNA and protein sequences

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5
Q

Mitochondria and chloroplast organelles were formed from

A

bacteria incorporated as endosymbionts into precursor eukaryotic cells

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6
Q

Which came first: mitochondria or chloroplast?

A

mitochondria

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7
Q

What are some features that cells share?

A

DNA, plasma membrane

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8
Q

How do cells differ?

A

differ in morphology, ability to move, internal organization (prokaryotes vs. eukaryotes), and metabolic activities

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9
Q

Eubacteria and Archaea have ___ genes than single-cell and multicellular eukaryotes

A

fewer

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10
Q

What is the use of E.coli?

A

E.coli is a model organism that is used to investigate common cell activities such as gene regulation and membrane transport found in other organisms

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11
Q

Diversity of function and morphology at the cellular and organismal levels, respectively, arises through

A

complex interactions of cellular products that have multiple functions (e.g. proteins, molecules, RNAs, etc.)

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12
Q

All cellular life is connected to a large degree as the result of

A

genetic conservation

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13
Q

What are the major cellular macromolecules?

A
  • amino acids
  • nucleic acids
  • carbohydrates
  • lipids
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14
Q

What are amino acids involved with?

A

proteins

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15
Q

What are nucleic acids involved with?

A

RNA and DNA

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16
Q

What are carbohydrates involved with?

A

structure or source of energy

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17
Q

What are lipids involved with?

A

structure (cell membranes) or energy source (fatty acids)

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18
Q

What are some important small molecules?

A
  • carbon-based molecules- carbon dioxide
  • water
  • ATP
  • ions and minerals
  • many others…
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19
Q

Prokaryote refers to

A

bacteria and archaea

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20
Q

Which came first: prokaryotic or eukaryotic cells?

A

prokaryotic; gave rise to eukaryotic

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21
Q

What does the Endosymbiont Theory state?

A

organelles in eukaryotic cells (mitochondria and chloroplasts) evolved from smaller prokaryotic cells

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22
Q

What are the two domains of prokaryotic cells?

A

Domain Archaea and Domain Bacteria

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23
Q

What types of organisms are in the Domain Archaea?

A
  • methanogens
  • halophiles
  • acidophiles
  • thermophiles
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24
Q

What is included in the Domain Bacteria?

A
  • mycoplasma (smallest known cells)

- cyanobacteria (some photosynthetic bacteria; gave rise to green plants and an oxygen rich atmosphere)

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25
Q

Archaea are often referred to as

A

extremophiles (because of the environment they live in and the materials they utilize for energy (sugar, ammonia, sulfur, hydrogen, metals))

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26
Q

What is characteristic of methanogens?

A

oxygen is poisonous to them

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27
Q

What is characteristic of halophiles?

A

live in high salt environments

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28
Q

What is characteristic of thermoacidophiles or thermophiles?

A

can’t survive at “low temperatures (55 C = 131 F)

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29
Q

Plasma cell contains prominent endoplasmic reticulum and Golgi complex organelles involved in

A

synthesizing antibodies secreted by the cell

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30
Q

What are some features of eukaryotic cells?

A
  • complex cytoskeletal system
  • organizations of DNA
  • DNA segregated in nucleus
  • specialized organelles for aerobic respiration and photosynthesis (mitochondria and chloroplasts)
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31
Q

What is the function of the complex cytoskeletal system in eukaryotic cells?

A
  • gives cell mechanical strength
  • controls cell shape
  • organizes cytoplasm
  • drives and guides movements
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32
Q

What is characteristic of the organization of DNA in eukaryotic cells?

A
  • long linear strands associated with proteins

- capable of condensing into mitotic chromosomes

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33
Q

What is characteristic of mitochondria and chloroplasts?

A
  • contain own DNA and protein synthesizing machinery
  • divide to increase number
  • believed to have come from prokaryotic cells engulfed by eukaryotic ancestor
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34
Q

What is the major difference in features of prokaryotic and eukaryotic cells in reference to cell membranes?

A
  • Bacteria and Eukaryotes: made of D-glycerol phospholipids

- Archaea: made of L-glycerol phospholipids with branching chains

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35
Q

What is the major difference in features of prokaryotic and eukaryotic cells in reference to cell walls?

A
  • Bacteria: made of peptidoglycan (combination of sugars and amino acids)
  • Archaea: made of S-layer, surface-layer proteins or pseudomurein (pseudopeptidoglycan)
  • Eukaryotes: cellulose (plants) or chitin (fungi)
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36
Q

Prokaryotes have ___ flagella while eukaryotes have ___ flagella

A

simple; complex

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37
Q

Prokaryotes move by

A

rotation

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38
Q

Eukaryotes move by

A

whip-like undulation

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39
Q

How is the rotating movement of bacteria different than that of archaea?

A

In bacteria, a proton gradient drives rotation; in archaea rotary motors are powered by ATP

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40
Q

What is another difference in bacteria, archaea, and eukaryotes?

A
  • Bacteria have a single circular DNA chromosome and no histone proteins
  • Archaea have a single circular DNA chromosome and histone-like proteins
  • Eukaryotes have multiple linear DNA chromosomes and histone proteins
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41
Q

A circular chromosome contains all necessary genes for

A

life function and replication

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42
Q

Plasmids contain extra genes that can

A

benefit survival

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43
Q

Archaea and eukaryotic histones share a common ancestry and

A

bind and wrap DNA similarly using conserved residues

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44
Q

What is the difference between eukaryotes and bacteria and archaea in reference to sexual reproduction?

A

Eukaryotes: sexual reproduction involving meiosis and fertilization
Bacteria and archaea: capable of exchanging pieces of DNA (conjugation) but no true sexual reproduction

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45
Q

Eukaryotes undergo

A

mitosis (nuclear division)

-utilizes a microtubule-containing spindle to separate duplicated chromosomes

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46
Q

Bacteria and archaea undergo

A

binary fission

-duplicated DNA separated by growth of cell membrane

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47
Q

What does phylogenetics state?

A

that many proteins in archaea are more closely related to eukaryotes than bacteria

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48
Q

Unicellular eukaryotic organisms range from relatively ___ (yeast) to perhaps the most ___ of all cells (protozoa and algae)

A

simple; complex

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49
Q

How many different cell types are found in the human body?

A

around 200

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50
Q

Multicellularity requires ___ and ___ adhesions

A

cell-to-cell; cell-to-matrix

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51
Q

Hox genes in conserved clusters encode highly conserved Hox protein master transcription factors, which control

A

the activities of other genes that direct the development of different segments along the head-to-tail axis in both protostomes and deuterostomes

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52
Q

Molecular complementarity enables proteins with complementary shapes and chemical properties to form

A

bimolecular interactions

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53
Q

Small molecule building blocks form

A

larger cellular structures and polymers such as DNA

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54
Q

T or F? Chemical reactions are reversible

A

T

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55
Q

What is K(eq)?

A

the ratio of forward (K(f)) and reverse (K(r)) reaction rate constants

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56
Q

What does K(eq) reflect?

A

the relative amounts of products and reactants at equilibrium

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57
Q

The energy driving many cellular activity reactions is derived from

A

hydrolysis of the high energy phosphoanhydride bond linking the beta and gamma phosphates in the ATP molecule

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58
Q

What does hydrophilic mean?

A

refers to molecules that readily dissolve in water; related to the polarity of the molecule (partial or full charge)

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59
Q

What does hydrophobic refer to?

A

molecules that of not readily dissolve in water; non polar molecules (can dissolve in organic solvents (non polar solvents))

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60
Q

What does amphipathic refer to?

A

biomolecules that exhibit both hydrophilic and hydrophobic regions

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61
Q

Bonds between atoms with shared pairs of electrons are called

A

covalent bonds

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62
Q

Stable combinations of atoms held together by covalent bonds

A

molecules

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63
Q

Molecules with more than one type of atom

A

compounds

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64
Q

Electrons are present around an atom’s nucleus in

A

“clouds” or orbitals that are roughly defined by their boundaries

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65
Q

A primary determinant of the chemical properties of an element

A

the number of outer-shell electrons

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66
Q

In covalent bonds, energy is released during

A

formation

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67
Q

T or F? Covalent bonds are stable under most conditions

A

T

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68
Q

The amount of energy required to break a bond is ___ as the amount of energy released when the bond is formed

A

the same

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69
Q

How many unpaired electrons are in carbon’s outer orbital?

A

4

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70
Q

Carbon can form ___ covalent bonds

A

4

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71
Q

In covalent bonds, the number of shared pairs contributes to

A

the shape of the molecule

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72
Q

The atoms around single bonds

A

rotate

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73
Q

The atoms around double or triple bonds

A

don’t rotate

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74
Q

Are polar bonds hydrophilic or hydrophobic?

A

hydrophilic

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75
Q

Polar molecules have ___ distributions of electrical charge

A

asymmetric

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76
Q

Are non polar bonds hydrophilic or hydrophobic?

A

hydrophobic

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77
Q

Non polar molecules lack

A

polarized bonds

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78
Q

Amphipathic molecules have both ___ and ___ regions

A

polar and nonpolar

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79
Q

What are some examples of amphipathic (having both polar and non polar regions) molecules?

A

proteins and phospholipids

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80
Q

Polarity or non polarity of biomolecules is determined by

A

the presence or absence of electronegative atoms within the molecular structure

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81
Q

What is electronegativity?

A

the ability of an atom to attract electrons towards itself forming a polar covalent bond

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82
Q

Hydrogen has one electron to share and forms __ covalent bond

A

1

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83
Q

Oxygen usually forms two covalent bonds but has

A

two additional pairs of electrons that can participate in non covalent interactions

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84
Q

Sulfur has up to __ electrons to share

A

6

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85
Q

Sulfur forms __ covalent bonds in hydrogen sulfide

A

2

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86
Q

Sulfur forms __ covalent bonds in sulfuric acid

A

6

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87
Q

Nitrogen has __ electrons to share

A

5

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88
Q

In ammonia (NH3), the nitrogen forms __ covalent bonds; the pair of electrons around the atom not involved in a covalent bond take part in ___

A

3; non covalent interactions

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89
Q

In the ammonium ion (NH4+), nitrogen forms 4 covalent bonds, which have a ___ geometry

A

tetrahedral

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90
Q

Phosphorous has __ electrons to share

A

5

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91
Q

Phosphorous commonly forms __ covalent bonds, as in phosphoric acid (H3PO4) and its phosphate derivatives

A

5

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92
Q

Phosphoric acid (H3PO4) and its phosphate derivatives

A

form the backbone of nucleic acids, high energy bonds in ATP, and covalently phosphorylate amino acid OH groups to regulate proteins activity

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93
Q

Carbon forms __ covalent bonds in many biologically relevant molecules

A

4

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94
Q

Carbon forms ___ in other non relevant molecules

A

‘unsaturated’ double bonds

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95
Q

What are functional groups?

A

groups of atoms giving organic molecules different characteristics and properties

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96
Q

What does the hydroxyl functional group look like?

A

-OH

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97
Q

What does the acyl functional group look like?

A

O
||
–C–R

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98
Q

What does the carbonyl functional group look like?

A

O
||
–C–

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99
Q

What does the carboxyl functional group look like?

A

O
||
–C–O^-

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100
Q

What does the sulfhydryl functional group look like?

A

–SH

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101
Q

What does the amino functional group look like?

A

–NH2 or –NH3+

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102
Q

What does the phosphate functional group look like?

A
O
       ||
--O--P--O^-
        |
       O^-
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103
Q

What does a pyrophosphate functional group look like?

A
O      O
        ||       ||
--O--P--O--P--
        |         |
       O^-   O^-
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104
Q

What does the ester functional group look like?

A

||
–C–O–C–
|

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105
Q

What does the ether functional group look like?

A

|
–C–O–C–
| |

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106
Q

What does the anide functional group look like?

A

O
||
–N–C–
|

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107
Q

Covalent bond electrons are shared unequally between atoms with different

A

electronegativities

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108
Q

What is a dipole moment?

A

when covalent bond electrons are shared unequally between atoms with different electronegativities

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109
Q

In a non polar covalent bond between atoms

A

the bonding electrons are shared equally between two atoms with similar electronegativity
(ex: C-C and C-H bonds)

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110
Q

In polar covalent bonds between atoms with different electronegativities,

A

shared electrons spend more time closer to the more electronegative atom resulting in partial negative and positive charges on each end of the molecule

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111
Q

Shared electrons stay closest to the nucleus with the highest

A

electronegativity

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112
Q

What is the extent of dipole charge separation?

A

dipole moment

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113
Q

A dipole moment is the product of

A

the partial charge on each atom and the distance between the two atoms

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114
Q

Bond strength/energy is

A

the energy required to break/make a particular type of bond

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115
Q

Covalent bonds are much __ and more __ than non covalent bonds

A

stronger; stable

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116
Q

Multiple non covalent interactions can combine to form strong associations in

A

macromolecules and structures such as DNA and membranes

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117
Q

The energy in the “high-energy” phosphoanhydride bonds in ATP used to power numerous cellular processes is __ than the energy associated with single (C-C) and double (C=C) bonds

A

less

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118
Q

Noncovalent bonds are __ than covalent bonds

A

much weaker

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119
Q

Non covalent are responsible for

A

the transient interaction between cellular macromolecules

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120
Q

What does multipoint contacts additive do?

A
  • produce stable structures
  • provide specificity in molecular interactions
    • selectivity in biological associations
    • conformation of macromolecules
    • formation of complexes between macromolecules
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121
Q

What are ionic bonds?

A

attractions between charged atoms

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122
Q

T or F? Ionic bonds are weakened in the presence of water

A

T

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123
Q

In solid crystals, cations and anions form neatly ordered arrays in which

A

the positive and negative charges counterbalance each other

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124
Q

The energy released in formation of ion hydration shells (energy of hydration) is greater than

A

the lattice energy that stabilizes the crystal

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125
Q

Increasing ion concentration can

A

compete for, weaken, or even disrupt the ionic interactions holding biomolecules together

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126
Q

When do hydrogen bonds occur?

A

when covalently bonded hydrogen has a partial positive charge and attracts electrons of a second atom

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127
Q

H-bonds determine

A

the structure and properties of water

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128
Q

Water forms hydrogen bonds with alcohols and amines, which

A

solubilizes compounds

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129
Q

The peptide group and ester group, which are present in many biomolecules form __ with water or other polar groups to stabilize molecular structures and interactions

A

hydrogen bonds

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130
Q

What are Van der Waals interactions?

A

hydrophobic attractions between non polar molecules that are due to transient dipole formation

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131
Q

Where do Van der Waals interactions take place?

A

between atoms that are close enough for electrons of one atom to overlap and perturb electrons of the other atom

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132
Q

Transient dipoles in the electron clouds of all atoms give rise to weak attractive forces between

A

a partial negative charge and a partial positive charge

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133
Q

What are hydrophobic interactions?

A

occurs when non polar molecules associate and minimize their exposure to polar molecules

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134
Q

Molecular complementary of two protein surface shapes, charges, polarity, and hydrophobicity permit multiple weak interactions that combined can form

A

specific, weak to strong, transient to stable interactions

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135
Q

What is Kd?

A

bonding dissociation constant

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136
Q

Induced fit binding of one molecule changing conformation of the other increases

A

molecular complementarity

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137
Q

What are the macromolecule polymers and their monomer subunits?

A

proteins-amino acids
nucleic acids-nucleotides
polysaccharides-monosaccharides

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138
Q

Differences in size, shape, charge, hydrophobicity, and reactivity of the 20 common amino acid side chains determine

A

protein chemical and structural properties

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139
Q

What are polysaccharides?

A

hexoses (glucose and others) linked by two types of bonds

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140
Q

What do nucleic acids do?

A

store and transmit genetic information

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141
Q

What do carbohydrates include?

A

simple sugars and sugar polymers

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142
Q

Lipids are a diverse group of __

A

non polar molecules

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143
Q

Fats are made of

A

glycerol linked by three ester bonds to three fatty acids

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144
Q

What causes a dehydration reaction?

A

the polymerization of two monomers by forming a covalent bond

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145
Q

What is the result of a dehydration reaction?

A

the loss of water

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146
Q

What are hydrolysis reactions responsible for?

A

the breakdown or cleavage of a covalent bond by incorporating water

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147
Q

Major types of biological macromolecules are assembled by __ __ of multiple small identical or similar molecules (monomers): amino acids-proteins, nucleotides-nucleic acids, and monosaccharides-polysaccharides

A

covalent (dehydration) polymerization

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148
Q

What are the components of amino acids?

A
  • an alpha carbon
  • an amine group
  • a carboxyl group
  • a variable R group
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149
Q

Amino acids are linked together by

A

peptide bonds into a polypeptide chain to make a protein

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150
Q

What determines the characteristic properties of each amino acid and is the basis for grouping the 20 common amino acids into three main categories: hydrophobic, hydrophilic, and special

A

The side chain (R group) of the amino acid

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151
Q

When an amino acid is hydrophobic what does that mean?

A

they have a non polar R group

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152
Q

What does it mean when an amino acid is labeled hydrophilic?

A

it has a polar R group and its ionic groups are charged at pH 7

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153
Q

What are examples of special amino acids?

A
  • C with reactive sulfhydryl group that can form disulfide bonds
  • G with single H that can fit into small spaces in proteins
  • P with cyclized R group that forms rigid kinks in proteins
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154
Q

Humans can synthesize __ amino acids, but __ essential amino acids must be consumed in diet

A

11;9

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155
Q

Amino acids in proteins may be

A

modified

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156
Q

Peptide bonds form between the __ and the __ of participating amino acids

A

alpha-carbonyl; alpha-amino

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157
Q

Amino acids differ in the __ attached to one of the bonds of the alpha-carbon

A

R group

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158
Q

R groups of amino acids can be

A

polar charged, polar uncharged, nonpolar

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159
Q

Polar charged contain R groups that

A

act as stronger organic acids, bases; can form ionic bonds

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160
Q

What are characteristics of polar charged amino acids?

A
  1. almost always fully charged at pH 7; side chains are relatively strong organic acids and bases
  2. Can form ionic bonds due to charges; histones with arginine (+- charge) bind to negatively charged phosphate groups of DNA
  3. Histidine- usually only partially charged at pH 7; often important in enzyme active sites due to its ability to gain or lose a proton in physiologic pH ranges
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161
Q

Polar uncharged amino acids contain

A

R groups that are weakly acidic or basic; not fully charged at pH 7

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162
Q

Polar uncharged amino acids can

A

form hydrogen bonds with other molecules like water since they have atoms with a partial negative or positive charge

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163
Q

What is characteristic of non polar amino acids?

A
  • R groups hydrophobic
  • generally lack O and N
  • can’t interact with water or form electrostatic bonds
  • vary primarily in size and shape
    • allows them to pack tightly into protein core
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164
Q

Non polar amino acids associate with one another via

A

hydrophobic and van der Waals interactions in protein core

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165
Q

What is unique about glycine (R=H)?

A

small R group makes backbone flexible and able to move so it is useful in protein hinges; small R group allows 2 backbones (of same or different protein) to approach closely

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166
Q

What is unique about proline?

A

R group forms ring with amino group (imino acid); hydrophobic amino acid that does not readily fit into orderly secondary structure (alpha-helix)

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167
Q

What is unique about cysteine?

A

R group has a reactive –SH; forms disulfide (-S-S-) bridge with other cysteines often at some distance away in polypeptide backbone

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168
Q

Glycine has only __ as its R group and is small

A

–H

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169
Q

The alpha-carbon of __ is part of a ring, creating kinks in the protein

A

proline

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170
Q

Cysteine forms __ __ (-S-S-) with other cysteines

A

disulfide bridges

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171
Q

The nature of the __ determines the function of the protein

A

R groups

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172
Q

Each nucleotide consists of what three parts?

A
  • 5 carbon sugar
  • a phosphate group
  • a nitrogenous base
    • bases are either purines or pyrimidines
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173
Q

A phosphate group is linked to the 5’ C in a pentose (five-carbon) sugar by

A

a phosphoester bond

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174
Q

A pentose (five-carbon) sugar is linked through its __ to a nitrogenous base

A

1’ C

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175
Q

The pentose sugar in RNA is

A

ribose

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176
Q

The pentose sugar in DNA is

A

deoxyribose

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177
Q

What are examples of purines?

A

adenine and guanine

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178
Q

What are examples of pyrimidines?

A

cytosine

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179
Q

Thymine is only found in

A

DNA

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180
Q

Uracil is only found in

A

RNA

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181
Q

Purine means

A

pair of fused rings

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182
Q

Pyrimidines means

A

single ring

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183
Q

Nucleic acids can be polymerized by the formation of __ to produce single-stranded polymers

A

phosphodiester bonds

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184
Q

The long chains of deoxynucleotides in the double helix of DNA are linked by

A

hydrogen bonds

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185
Q

To link A to T, __ hydrogen bonds are needed

A

2

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186
Q

To link G to C, __ hydrogen bonds are needed

A

3

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187
Q

GC-rich DNA is

A

more stable

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188
Q

Nucleosides consist of a nitrogenous base covalently attached to

A

a sugar

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189
Q

Nucleotides consist of a nitrogenous base covalently attached to

A

a sugar (ribose or deoxyribose) and one to three phosphate groups

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190
Q

Carbohydrates include

A

simple sugars and sugar polymers

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191
Q

Carbohydrates serve as

A

energy storage molecules or structural molecules

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192
Q

What is the chemical structure of carbohydrates?

A

(CH2O)n

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193
Q

T or F? The sugars of carbohydrates can be linear but sometimes form ring structures

A

T

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194
Q

Ketose sugars

A

have a carbonyl (C=O) on an internal carbon

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195
Q

Aldose sugars

A

have a carbonyl (C=O) on a terminal carbon

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196
Q

Carbohydrates have a backbone of carbon linked by

A

single bonds

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197
Q

Usually __ and __ are attached to each carbon in the backbone of a carbohydrate

A

H; OH

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198
Q

Glycosidic bonds are __ links between sugars

A

-C-O-C-

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199
Q

Disaccharides are used as

A

a source of readily available energy

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200
Q

Where are oligosaccharides found?

A

bound to cells surface proteins and lipids

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201
Q

Oligosaccharides may be used

A

for cell recognition

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202
Q

Storage polysaccharides are

A

polymers of sugars joined by glycosidic bonds linked by alpha(1-4) linkage with branches consisting of alpha(1-6) linkages

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203
Q

Glycogen is

A

an animal product

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204
Q

Glycogen is made of

A

branched glucose polymers

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205
Q

Starch is

A

a plant product

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206
Q

Starch is made of

A

both branched and unbranched glucose polymers

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207
Q

What is cellulose?

A

structural polysaccharides comprised of beta(1-4)-linked glucose units

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208
Q

What is chitin?

A

structural polysaccharides found in the exoskeleton of invertebrates

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209
Q

Lipids are a diverse group of

A

non polar molecules

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210
Q

Fats may be made of

A

glycerol linked by three ester bonds to three fatty acids

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211
Q

Fatty acids are

A

unbranched hydrocarbons with one carboxyl group that are amphipathic

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212
Q

Saturated fatty acids

A

lack C=C double bonds and are solid at room temperature

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213
Q

Unsaturated fatty acids

A

have one or more C=C double bonds and are liquid at room temperature

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214
Q

Steroids are

A

animal lipids derived from cholesterol

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215
Q

Phospholipids are

A

amphipathic lipids that are a major component of cell membranes

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216
Q

Diacylglycerols consist of

A
  • glycerol backbone
  • 2 fatty acids
  • phosphate group
  • small polar group
    • nomenclature based on polar group
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217
Q

K(eq) = product/reactant ratio when forward and reverse rates are

A

equal

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218
Q

Cell linked reactions are at a steady state, not

A

equilibrium

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219
Q

The dissociation constant (K(d)) is a measure of

A

non covalent interactions

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220
Q

The pH range of cytoplasm is

A

7.2-7.4

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221
Q

The pH of some organelles such as lysosomes is

A

4.5

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222
Q

Acids __ protons (H+)

A

release

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223
Q

Bases __ protons (H+)

A

bind

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224
Q

Biological systems use weak acid/base buffers to

A

maintain pH in narrow ranges

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225
Q

The __ and __ at which chemical reactions proceed determine the chemical composition of cells

A

extent; rate

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226
Q

Chemical reactions are

A

reversible

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227
Q

Initial forward and reverse reaction rates depend on the

A

initial concentrations of reactants and products

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228
Q

The net forward reaction rate __ as the concentration of reactants decreases

A

slows

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229
Q

The net reverse reaction rate __ as the concentration of products increases

A

increases

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230
Q

What is characteristic of equilibrium?

A

the rates of the forward and reverse reactions are equal, and the concentrations of reactants and products remain constant

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231
Q

What is the equilibrium constant (K(eq))?

A

the ratio of product to reactant concentrations at equilibrium and the ratio of forward to reverse rate constants

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232
Q

Equilibrium constant depends on what?

A

temperature and pressure

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233
Q

A catalyst can increase reaction rate but has no effect on

A

equilibrium constant (K(eq))

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234
Q

When K(eq) = 1,

A

the reaction is at equilibrium

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235
Q

Cells must maintain a __ __ for the biochemical reactions

A

steady state

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236
Q

Equilibrium results in

A

cell death

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237
Q

The concept of equilibrium also applies to the binding of one molecule to another without __ __ to either molecule

A

covalent changes

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238
Q

The dissociation constant K(d)) is the __ of the equilibrium constant

A

reciprocal

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239
Q

The dissociation constant (K(d)) is a measure of

A

the bonding affinity the two molecules have for one another

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240
Q

The lower the dissociation constant (K(d)), the __ the bonding affinity between two molecules

A

stronger

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241
Q

The higher the dissociation constant (K(d)), the __ the bonding affinity between two molecules

A

weaker

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242
Q

Macromolecules can have distinct __ __ for multiple ligands

A

binding sites

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243
Q

Acids __ protons

A

release

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244
Q

Bases __ protons

A

accept

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245
Q

Amphoteric molecules can act as

A

either acids or bases

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246
Q

What is the formula for pH?

A

pH = pKa + log([A-]/[HA])

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247
Q

Biological processes are sensitive to

A

pH

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248
Q

Changes in pH affect the __ __ and __ of proteins

A

ion state; function

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249
Q

__ in living systems resist changes in pH

A

buffers

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250
Q

What is the formula for pKa?

A

pKa = -logKa

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251
Q

What is the pKa of an acid?

A

the pH at which half the molecules are dissociated and half are neutral (undissociated)

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252
Q

pH is the major factor in determining if a macromolecule will be predominantly __, which in turn influences the types of __ interactions that may occur

A

ionized; noncovalent

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253
Q

If pKa - pH = 0, then

A

50% of the molecule is ionized and 50% is non-ionized

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254
Q

For weak acids, if the pH is higher than the pKa, then

A

more of the molecule is ionized than non-ionized

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255
Q

For weak acids, if the pH is lower than the pKa, then

A

less of the molecule is ionized than non-ionized

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256
Q

For weak bases, if the pH is lower than the pKa, then

A

more of the molecule is ionized than non-ionized

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257
Q

For weak bases, if the pH is higher then the pKa, then

A

less of the molecule is ionized than non-ionized

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258
Q

Ionized molecules can form

A

ionic bonds

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259
Q

Non-ionized molecules can form

A

hydrogen bonds or hydrophobic interactions

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260
Q

How do weak acids differ from weak bases?

A

-for weak acids:
pKa - pH = log ([nonionized]/[ionized])
-for weak bases:
pKa - pH = log ([ionized]/[nonionized])

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261
Q

Buffering capacity depends on

A

concentration of the buffer and the relationship between its pKa value and the pH

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262
Q

Buffers are best when they’re __ unit above or below pKa value

A

1

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263
Q

What does deltaG measure?

A

reaction change in free energy

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264
Q

-deltaG reactions are

A

thermodynamically favorable

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265
Q

+deltaG reactions are

A

not thermodynamically favorable

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266
Q

What is the equation for deltaG?

A

-2.3RTlogK(eq)

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267
Q

Rate of reaction depends on

A

activation energy

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268
Q

Rate of reaction lowered by a

A

catalyst

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269
Q

What is the ultimate source of all cell energy?

A

sunlight energy captured by photosynthesis

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270
Q

What is bioenergetics?

A

the study of the various types of energy transformations that occur in living organisms

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271
Q

What is energy?

A

capacity to do work, or the capacity to change or move something

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272
Q

What is thermodynamics?

A

the study of the changes in energy that accompany events in the universe

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273
Q

Kinetic energy is the energy of

A

movement

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274
Q

What is thermal energy?

A

the flow of energy from a region of higher temp to lower temp

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275
Q

Is thermal energy a major player in cellular activity?

A

no

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276
Q

What is radiant energy?

A

kinetic energy of photons or waves of light

e.g. photosynthesis

277
Q

What is mechanical energy?

A

the major form of kinetic energy in biology

e.g. reorganization of the cytoskeleton

278
Q

What is electric energy?

A

energy of moving electrons or charged particles

e.g. transport of charged ions across the cell membrane, electrically active neurons

279
Q

Potential energy is

A

stored energy

280
Q

What is chemical potential energy?

A

energy stored in bonds connecting atoms in molecules

e.g. conversion of glucose to ATP and NADH

281
Q

What are concentration gradients?

A

potential energy created by storing molecules on one side of a membrane and allowing them to flow across the membrane barrier spontaneously
e.g. oxidative phosphorylation

282
Q

What is electric potential energy?

A

potential energy produced by separating differently charged ions on opposite sides of the membrane, e.g. membrane potential

283
Q

What does the first law of thermodynamics state?

A

energy can neither be created nor destroyed

284
Q

The first law of thermodynamics is called

A

the law of conservation of energy

285
Q

What is transduction?

A

conversion of energy from one form to another

286
Q

What is an example of transduction?

A

conversion of sunlight into chemical energy

287
Q

The universe can be dividd into

A

system and surroundings

288
Q

What is the system?

A

a subset of the universe under study

289
Q

What are the surroundings?

A

everything that is not part of the system

290
Q

The energy of the system is called

A

internal energy (E)

291
Q

The change of the energy of the system during a transformation is called

A

deltaE

292
Q

What is the equation for the first law of thermodynamics?

A

deltaE = Q - W
E: internal energy
Q: heat energy
W: work energy

293
Q

When there is energy transduction (deltaE) in a system, heat content may

A

increase or decrease

294
Q

Reactions that lose heat are

A

exothermic

295
Q

Reactions that gain heat are

A

endothermic

296
Q

The first law predicts whether an energy change will be positive or negative

A

F

297
Q

What does the second law of thermodynamics state?

A

events in the universe tend to proceed from a state of higher energy to a state of lower energy toward equilibrium

298
Q

When an event is spontaneous, it means that

A

it can occur without the input of external energy

299
Q

Loss of available energy during a process is the result of

A

a tendency for randomness to increase whenever there is a transfer of energy

300
Q

Events progress from

A

an ordered state to a disordered state

301
Q

What is entropy?

A

a measure of the randomness of disorder

302
Q

Every event is accompanied by __ __ in the entropy of the universe

A

an increase

303
Q

Entropy is associated with

A

random movements of particles or matter

304
Q

Living systems maintain

A

a state of order, or low entropy

305
Q

T or F? Entropy is energy not available to do additional work

A

T

306
Q

What is the equation for loss of available energy?

A

TdeltaS

deltaS: change in entropy

307
Q

Entropy (disorder) will increase until

A

the system reached equilibrium

308
Q

Spontaneous reactions are thermodynamically

A

favorable

309
Q

The second law of thermodynamics is only absolute in

A

a closed system

310
Q

Catabolic pathways are

A

metabolic pathways that break down molecules into smaller units and release energy

311
Q

Anabolic pathways are

A

metabolic pathways that construct molecules from smaller units and require energy

312
Q

Cellular metabolism is __ metabolism

A

non-equilibrium

313
Q

Cells are __ thermodynamic systems

A

open

314
Q

Cellular metabolism exists in a

A

steady state

315
Q

What are the characteristics of a steady state?

A
  • concentrations of reactants and products remain constant, but not at equilibrium
  • New substrates enter and products are removed
316
Q

What is the difference between equilibrium and steady-state metabolism?

A

maintaining a steady state requires a constant input of energy, whereas maintaining equilibrium does not

317
Q

What is the equation of enthalpy?

A

deltaH (enthalpy) = deltaG + TdeltaS

318
Q

Free energy, deltaG is

A

the energy available to do work

319
Q

The spontaneity of a reaction is

A

deltaG

320
Q

If deltaG is <0, then the reaction is

A

exergonic

321
Q

If deltaG is >0, then the reaction is

A

endergonic

322
Q

Spontaneity depends on both

A

enthalpy and entropy

323
Q

What is Gibbs equation?

A

deltaG = deltaH -TdeltaS

  • deltaG: change in free energy of system
  • deltaH: change in enthalpy; total energy content of a system
  • T: temp
  • deltaS: change in entropy; an increase in disorder
324
Q

A reaction is energetically favorable if deltaG is

A

negative

325
Q

A reaction that is -deltaG

A

will proceed spontaneously

326
Q

A reaction with a negative deltaG is an ___ reaction

A

exergonic

327
Q

A reaction with a negative deltaG is thermodynamically

A

favorable

328
Q

In a reaction with a negative deltaG

A

total free energy of the reactants is greater than the total free energy of the products

329
Q

The greater the deltaG of a reaction,

A

the farther the reaction is from equilibrium and the more work that can be performed by the system

330
Q

If a reaction has a positive deltaG, it is energetically

A

unfavorable

331
Q

A reaction with a positive deltaG is an ___ reaction

A

endergonic

332
Q

Reactions with a positive deltaG

A

require the input of energy to proceed

333
Q

In exergonic reactions (spontaneous), the free energy of the products is

A

less than that of the reactants and energy is released as the reaction proceeds

334
Q

In endergonic reactions (not spontaneous), the free energy of the products is

A

greater than that of the reactants and requires an external energy source

335
Q

In the equation deltaG = deltaH - TeltaS, if deltaH is positive (+) and deltaS is negative (-), the reaction is

A

not spontaneous and energetically unfavorable

336
Q

In the equation deltaG = deltaH - TdeltaS, if deltaH is negative (-) and deltaS is positive (+), the reaction is

A

spontaneous and energetically favorable

337
Q

In the equation deltaG = deltaH - TdeltaS, if BOTH deltaH and deltaS are negative (-), the reaction is

A

not spontaneous

338
Q

In the equation deltaG = deltaH - TdeltaS, if BOTH deltaH and deltaS are positive (+), the reaction is

A

not spontaneous

339
Q

The rates of chemical reactions are proportional to

A

the concentration of reactants

340
Q

At equilibrium, the free energies of the products and reactants are

A

equal (deltaG = 0)

341
Q

Reactions with a Keq > 1 have a __ deltaG

A

negative

342
Q

Reactions with a Keq < 1 have a __ deltaG

A

positive

343
Q

Reactions with a Keq = 1 have a delta G of

A

0

344
Q

deltaG is influenced by

A

the concentration of molecules in the reaction

345
Q

Equilibrium constant (K(eq)) equals

A

[products]/[reactants]

346
Q

If K(eq) > 1

A

forward reaction favored

347
Q

If K(eq) < 1

A

reverse reaction favored

348
Q

If K(eq) = 1

A

forward and reverse reactions are equally favored (equilibrium)

349
Q

How does a catalyst increase the speed of a reaction?

A

lowers the activation energy of the reaction

350
Q

Catalysis does not influence the __ of a reaction

A

thermodynamics

351
Q

Cellular reactions with a positive (+) deltaG occur because

A
  1. the ratio of reactants to products is kept low enough to drive forward reaction
  2. input of energy; coupled reactions
  3. use activated carrier molecules
352
Q

NADH, NADPH, and FADH2 are

A

electron carriers

353
Q

Redox reactions involve the

A

transfer of electrons from one molecule (oxidation) to another molecule (reduction)

354
Q

In a redox reaction, electrons move spontaneously toward atoms or molecules having

A

more positive reduction potentials

355
Q

Non equilibrium conditions are maintained because

A

cell is an open system

356
Q

The exceptional conformational flexibilities of disordered proteins contribute to

A

their multiple functions

357
Q

Homologous proteins

A
  • evolved from a common ancestor
  • have similar sequences, structures and functions
  • can be classified into families and superfamilies
358
Q

The human genome has __ protein-encoding genes

A

20,000-23,000

359
Q

What is the primary structure of proteins?

A

linear sequence of amino acids linked by peptide bonds

360
Q

What is the secondary structure of proteins?

A

folding of the polypeptide chain into local alpha-helices or beta-sheets

361
Q

What is the tertiary structure of proteins?

A

peptide 3D shape

  • structure of a peptide composed of secondary structural elements and various loops and turns
  • may form distinct, independently stable domains
362
Q

What is the quaternary structure of proteins?

A

association into multipoeptide complexes

-some functional proteins are composed of more than one polypeptide

363
Q

What is characteristic of supramolecular complexes?

A

can be very large, consisting of tens to hundreds of subunits

364
Q

Protein functions depend on

A

specific binding interactions and conformational changes in the structure of a properly folded protein

365
Q

How are proteins involved in structure?

A

they are involved in organizing the genome, organelles, cytoplasm, protein complexes, and membranes in 3D space

366
Q

How are proteins involved in regulation?

A

the control protein activity

367
Q

How are proteins involved in signaling?

A

they monitor the environment and transmit information

368
Q

How are proteins involved in transport?

A

they move small molecules and ions across membranes

369
Q

How are proteins involved in enzyme activity?

A

they catalyze chemical reactions

370
Q

How are proteins involved in motors?

A

they generate force for movement

371
Q

The 3D structure of a protein is determined by

A

the amino acid sequence and intramolecular non covalent interactions

372
Q

How is a peptide bond formed?

A

a dehydration reaction linking one amino acid C-terminus to another amino acid N-terminus

373
Q

What is characteristic of a polypeptide?

A

linear polymer has a free amino end (N-terminus) and a free carboxyl end (C-terminus)

374
Q

Peptide bonds link

A

the amino nitrogen atom of one amino acid with the carbonyl carbon atom of an adjacent amino acid in the chain

375
Q

If there is a change in an amino acid due to a point mutation, the affect on the structure depends on

A

the nature of the side chain

  • may have little or no affect if side chain has similar properties
  • more affect if side chain has different properties
376
Q

A change in an amino acid has a greater impact if

A

the change causes a change in the 3D structure or properties

377
Q

Secondary structure riders to the conformation of adjacent amino acids into

A

an alpha-helix, beta-sheet, hinges, turns, loops, or finger-like extensions

378
Q

What is a secondary structure?

A

stable spatial arrangement od polypeptide chain segments held together by hydrogen bonds between backbone amide and carbonyl groups

379
Q

A polypeptide backbone (ribbon) folds into a spiral/helix with

A

3.6 amino acids per turn

380
Q

An alpha-helix is stabilized by

A

hydrogen bonds between backbone oxygen and hydrogen atoms (more bonds-more stable)

381
Q

R groups project outward from the surface of the alpha-helix and

A

determine the chemical nature of helix faces

382
Q

Pralines can’t participate in hydrogen bonding and are usually excluded from

A

an alpha-helix

383
Q

What is a beta sheet?

A

laterally packed beta strands, each of which is a nearly fully extended polypeptide segment

384
Q

A three-stranded beta sheet is made of

A

antiparallel beta strands with connection loops

-alternate R groups project above and below the plane of the sheet

385
Q

Three-stranded are stabilized by

A

hydrogen bonds between backbone oxygen and hydrogen atoms in amino acids on different strands

386
Q

Alpha carbon bond angles produce

A

a pleated polypeptide backbone contour

387
Q

A parallel beta strand sheet is composed of

A

the same N-to-C strand orientations with connecting loops

388
Q

What is the structure of a beta turn?

A
  • composed of four residues
  • reverses direction of a polypeptide chain (180 U-turn)
  • Calpha carbons of the first and fourth resides are usually less than 0.7nm apart and are linked by a hydrogen bond
  • glycine (smallest R group) and proline (built in bend) are commonly found in beta turns
389
Q

Structure dictates

A

function

390
Q

Beta turns facilitate

A

the folding of long polypeptides into compact structures

391
Q

Tertiary structure is the conformation of

A

the entire polymer

392
Q

Tertiary structures are stabilized by

A
  • hydrophobic and Van der Waals interactions between non polar side chains
  • hydrogen bonds involving polar side chains and backbone amino and carboxyl groups
393
Q

Proteins can be

A

fibrous or globular

394
Q

Hydrophobic residues of a tertiary structure

A

cluster together like drops of oil in the folded protein core, driven away from the aqueous surrounding by the hydrophobic effect

395
Q

Charged and uncharged polar side chains of the tertiary structure

A

form stabilizing interactions with surrounding water and ions on the protein surface

396
Q

Disulfide bonds between cysteine residues can also play a role in

A

stabilizing tertiary structure

397
Q

The formation of non covalent bonds results in

A

a release in energy and a more stable macromolecular structure (lower energy state)

398
Q

Proteins fold into a 3D shape that

A

requires the least amount of energy to maintain

399
Q

What are characteristics of globular proteins?

A
  • generally water-soluble
  • compactly folded structure
  • often but not exclusively spheroidal in shape
400
Q

What are characteristics of fibrous proteins?

A
  • large
  • elongated
  • often stiff molecules
401
Q

What is characteristic of integral membrane proteins?

A

embedded within the phospholipid bilayer of membranes

402
Q

Globular, fibrous, and integral membrane proteins are all

A

well-ordered proteins

403
Q

What are characteristics of intrinsically disordered proteins?

A
  • do not have well ordered structures in their native states
  • polypeptide chains are very flexible with no fixed conformation
  • interact with multiple partner proteins
  • only fold into a well-defined conformation during specific interaction with other protein partners
404
Q

What is characteristic of induced fit?

A

the interaction between two molecules results in conformational changes that allow the molecules to interact with greater affinity for one another

405
Q

Calpha backbone traces depict

A

how the polypeptide is tightly packed into a small volume

406
Q

Ball-and-stick representations reveal

A

locations of all atoms

407
Q

Ribbon diagrams emphasize

A

how beta-strands and alpha-helices are organized in the protein

408
Q

Water-accessible surface models reveal

A

protein surface topology with positive charge and negative charge regions

409
Q

What are structural motifs?

A

regular combinations of secondary structures usually with a specific type of function

410
Q

Structural motifs can be encoded by

A

a highly conserved sequence motif

411
Q

What is a coiled-coil motif?

A

two alpha helices wound around each other

412
Q

What is an EF hand?

A

a type of helix-loop-helix motif in many proteins, including many calcium-binding and DNA-binding regulatory proteins

413
Q

Zinc-finger motifs are present in

A

many DNA-binding proteins that help regulate transcription

414
Q

Domains occur when

A

proteins are composed of two or more distinct regions

415
Q

What are the three main classes of protein domains?

A

functional, structural, and topological domain

416
Q

What is the functional domain of a protein?

A

region of protein that exhibits a specific activity, usually independent of other regions of the protein

417
Q

What is the structural domain of a protein?

A

region of >40 amino acids arranged in a single, stable, distinct structure often comprised of one or more secondary structures

418
Q

What is the topological domain of a protein?

A

regions of proteins defined by their spatial relationship to the rest of the protein; e.g., membrane spanning proteins have extracellular, membrane embedded and cytoplasmic domains

419
Q

Well-ordered proteins easily fold into their

A

proper 3D shape

420
Q

75% of eukaryotic proteins have multiple

A

structural domains

421
Q

What is epidermal growth factor (EGF) precursor generated by?

A

proteolytic cleavage

422
Q

Proteolytic cleavage generates multiple

A

EGFs (epidermal growth factors)

423
Q

What is Neu?

A

EGF domain plus other domains

424
Q

What is Tissue plasminogen activator (TPA)?

A

EGF domain plus other domains

425
Q

Quaternary structure refers to proteins composed of

A

subunits

426
Q

Quaternary structure refers to

A

the manner in which subunits interact

427
Q

Different proteins can become physically associated to form

A

a multiprotein or supramolecular complexes

428
Q

Protein amino acid sequence determines its

A

3D structure and function

429
Q

ATP-dependent molecular chaperones and chaperonins assist

A

protein folding in vivo

430
Q

Misfolded/denatured proteins can form well-organized amyloid fibril aggregates that can

A

cause diseases

431
Q

Polypeptide chain on either side of the peptide bond can be oriented in either a __ or __ configuration relative to the peptide bond

A

trans; cis

432
Q

99.97% of the peptide bonds that have any residue other than proline at P2 are in the __ configuration

A

trans

433
Q

Planar peptide bonds limit

A

the shapes into which proteins can fold

434
Q

In peptide bonds, the carbonyl carbon and amide nitrogen must

A

lie in a fixed plant

-little rotation of the peptide bond is possible

435
Q

The only flexibility in a polypeptide chain is

A

rotation of the fixed planes of adjacent bonds

436
Q

Proteins may assume their __ conformation through a series of steps

A

native

437
Q

What is the monomeric protein folding hierarchy?

A

primary –> secondary –> tertiary –> structure

438
Q

Formation of small structural motifs appears to precede formation of __ and the __

A

domains; final tertiary structure

439
Q

Domain folding is usually independent of

A

other regions of the protein

440
Q

What is the native state of a protein?

A

usually the conformation with the lowest free energy (G)

441
Q

What are molecular chaperones?

A

“helper proteins” that prevent nonselective interactions during protein folding to achieve proper 3D conformation

442
Q

What do molecular chaperones do?

A

bind to a short segment of a protein substrate and stabilize unfolded or partly folded proteins, preventing aggregation or degradation

443
Q

Chaperonins allow

A

large new proteins to assemble without interference from other macromolecules

444
Q

Chaperonins process up to __ of the cells’ proteins

A

15%

445
Q

The Hsp70 chaperone protein cycle

A

binds transiently to a nascent polypeptide as it emerges from a ribosome or to a protein that has unfolded

446
Q

What is the first step of the Hsp70 chaperone protein cycle?

A

Hsp70 binds unfolded protein in rapid equilibrium to the open conformation of the substrate-binding domain and ATP in the nucleotide-binding domain

447
Q

What is the second step of the Hsp70 chaperone protein cycle?

A

Co-chaperone accessory proteins (DnaJ/Hsp40) stimulate ATP hydrolysis inducing a large conformational change in the substrate-binding domain that locks the unfolded protein region into the substrate-binding domain- proper folding is facilitated

448
Q

What is the third step of the Hsp70 chaperone protein cycle?

A

exchange of ATP for the bound ADP stimulated by other accessory co-chaperone proteins (GrpE/BAG1)

449
Q

What is the fourth step of the Hsp70 chaperone protein cycle?

A

Releases the properly folded substrate, regenerating the open conformation

450
Q

What are the steps of the Hsp90 molecular chaperone cycle?

A
  1. no nucleotide bound to the nucleotide-binding domain- dimer in a very flexible, open configuration that can bind a client
  2. rapid ATP binding causes conformational change- nucleotide-binding domains dimerize and the substrate-binding domains move together
  3. intermediate state
  4. closed conformation
  5. ATP hydrolysis- conformational change in Hsp90 that may include a highly compact form, folding of the client, and client protein release
  6. release of ADP regenerated the initial flexible open state
451
Q

What are chaperonins?

A

folding chambers into which all or part of an unfolded protein can be bound in an appropriate environment, giving it time to fold properly

452
Q

Proline isomerases catalyze

A

the cis/trans isomerization to facilitate protein folding

453
Q

Cis/trans isomerization of a single proline

A
  • alters structure of a protein domain
  • can influence a protein’s activity
  • proline isomerases may act as switches that regulate protein activity
454
Q

T or F? All amino acids are in every protein

A

F

455
Q

The defined and predictable structure of proteins based on

A
  • nature of amino acids in protein
  • order of amino acids
  • environment
456
Q

Misfolded proteins/proteolytic fragments can accumulate as __ inside or outside of cells in various organs including joints between bones, the liver, and the brain

A

aggregates or plaques

457
Q

Many diverse proteins can aggregate into amyloid (well-ordered) __ that have a common structure and can cause amyloidoses diseases such as Alzheimer’s, Parkinson’s, and “mad cow” disease

A

fibrils

458
Q

Protein function depends on

A

binding other molecules (ligands)

459
Q

Enzymes accelerate rate of cellular reactions by

A

lowering activation energy and stabilizing transition-state intermediates

460
Q

Enzymes often use __ mediated by one or more amino acid side chains

A

acid-base catalysis

461
Q

Metabolic pathway enzymes may be associated as

A
  • domains of a monomeric protein
  • subunits of a multimeric protein
  • components of a protein complex assembled on a common scaffold
462
Q

What is a ligand?

A

molecule to which a protein binds

463
Q

Ligand binding often results in

A

a conformation change in the protein’s 3D shape

464
Q

What is specificity?

A

the ability of a protein to bind one molecule or a small group of molecules in preference to all other molecules

465
Q

What is affinity?

A

refers to the tightness or strength of binding determined by the ligand-binding site

466
Q

Low Kd = __ affinity

A

high

467
Q

High Kd = __ affinity

A

low

468
Q

__ __ is required for specificity and affinity

A

molecular complementarity

469
Q

What are CDR’s? What are they responsible for?

A

complementarity-determining regions; responsible for the specificity of ligand binding

470
Q

Enzymes are almost always

A

proteins

471
Q

What are ribozymes?

A

RNA molecules with enzymatic activity

472
Q

Enzymes may be conjugated with

A

non-protein components

473
Q

What are cofactors?

A

inorganic enzyme conjugates (e.g., metals)

474
Q

What are coenzymes?

A

organic enzyme conjugates

475
Q

K(eq) and deltaG don’t predict the rates of reactions, only the

A

direction

476
Q

Enzymes are

A

biological catalysts

477
Q

Enzymes are present in cells in

A

small amounts

478
Q

Enzymes are __ altered during a reaction

A

reversibly

479
Q

Enzymes enter and exit a reaction

A

in the same condition

480
Q

T or F? Enzymes can only be used once in a reaction

A

F; can be used over and over

481
Q

Enzymes have __ effect on thermodynamics of reaction

A

no

482
Q

Enzymes increase __ of reaction

A

velocity

483
Q

Enzymes are highly specific for their particular reactants called

A

substrates

484
Q

Enzymes produce only

A

appropriate metabolic products

485
Q

T or F? Enzymes can be regulated to meet the needs of the cell

A

T

486
Q

Thermodynamically favorable reactions don’t proceed on their own at relatively rapid rates

A

in the absence of enzymes

487
Q

T or F? Kinetic stability and thermodynamic stability are not interdependent

A

T

488
Q

What is activation energy?

A

the energy that must be overcome for a chemical reaction to occur

489
Q

Chemical transformations require the breaking of

A

covalent bonds

490
Q

Reactants must contain sufficient __ to overcome activation energy and reach an activated state to achieve the atomic rearrangements necessary for a reaction to occur

A

kinetic energy

491
Q

The geometry and electron distribution of atoms around bonds are

A

distorted

492
Q

Shape of molecule distorted to

A

break the covalent bonds

493
Q

What is a transition state?

A

the point at which reactants reach the energy crest and are ready to be converted into products

494
Q

T or F? Activation energy isn’t required if the reaction is energetically favorable

A

F

495
Q

The activation energy required to reach the transition state is not a fixed value but varies with

A

the particular reaction mechanism utilized

496
Q

An enzyme interacts with its substrate to form

A

an enzyme-substrate (ES) complex

497
Q

The substrate binds to a portion of the enzyme called the

A

active site

498
Q

The active site and the substrate have ___ shapes that allow substrate specificity

A

complementary

499
Q

Enzymes catalyze reactions by making or breaking

A

substrate covalent bonds

500
Q

What does the substrate-binding pocket do?

A

binds specific substrates

501
Q

What does the catalytic site contain?

A

side chains of the catalytic amino acids that alter covalent bonds

502
Q

Catalytic and substrate-binding sites may

A

overlap or be in two structurally distinct regions

503
Q

Amino acids lining the side-chain-specificity pocket determine its

A

shape and charge and binding properties

504
Q

What does Trypsin do?

A

binds substrate (+) charged arginine and lysine side chains

505
Q

What does Chymotrypsin do?

A

binds large, hydrophobic side chains such as phenylalanine

506
Q

What does Elastase do?

A

binds small side chains such as glycine and alanine

507
Q

What are some mechanisms of enzyme catalysis?

A

substrate orientation, changing substrate reactivity, inducing strain in the substrate

508
Q

What is substrate orientation?

A

multiple substrates brought together in correct orientation to catalyze reaction

509
Q

What happens when you change substrate reactivity?

A

substrate influenced by amino acid side chains at active site that alter chemical properties (e.g., charge) of substrate

510
Q

What happens when you induce strain in the substrate?

A

enzyme changes conformation of substrate to bring closer to conformation of transition state

  • shifts in the conformation cause an induced fit between enzyme and substrate
  • covalent bonds of the substrate are strained
511
Q

What are the steps of the schematic model of an enzyme’s reaction mechanism?

A
  1. enzyme’s substrate-binding site and catalytic site cooperate in multistep reaction to convert substrate to product
  2. enzyme binds substrate molecules at a fixed enzyme active site
  3. Enzyme-substrate (ES) complex:
    - in equilibrium with the unbound enzyme and substrate
    - intermediate step in the conversion of substrate to product (P)
512
Q

Describe enzyme catalysis in multiple discrete steps

A
  1. initial formation of an ES complex
  2. conversion via a single transition state to the free enzyme and product
  3. activation energy for each step is significantly less than the activation energy for the uncatalyzed reaction, enhancing the reaction rate
513
Q

What is kinetics?

A

the study of rates of enzymatic reactions under various experimental conditions

514
Q

Rates of enzymatic reactions increases with __ until the enzyme is saturated

A

increasing substrate concentrations

515
Q

At saturation, every enzyme is working at

A

maximum capacity

516
Q

The velocity at saturation is called

A

maximal velocity (V(max))

517
Q

What is the turnover number?

A

the number of substrate molecules converted to product per minute per enzyme molecule at V(max)

518
Q

What is Michaelis constant (K(m))?

A

the substrate concentration [S] that yields a half-maximal reaction rate; depends on affinity of enzyme for substrate

519
Q

Maximal reaction velocity (V(max)) depends on

A

number of enzymes

520
Q

What happens when you quadruple enzyme concentration?

A
  • V(max) increases proportionally

- K(m) remains the same

521
Q

Acid-base catalysis is __ dependent

A

pH

522
Q

Catalysis requires a particular ionization state (protonated or nonprotonated) of

A

one or more amino acid side chains in the catalytic site

523
Q

Enzyme activity is influenced by

A

temp

524
Q

How can temperature affect an enzyme?

A
  • introduce energy to the system and increase kinetic activity
  • affect the 3D structure of the enzyme since high temperatures can disrupt ordered structures in proteins
525
Q

What do enzyme inhibitors do?

A

slow the rates for enzymatic reactions

526
Q

Irreversible inhibitors bind __ to the enzyme

A

tightly

527
Q

Reversible inhibitors bind __ to the enzyme

A

loosely

528
Q

Competitive inhibitors compete with the enzyme for

A

active sites

529
Q

Competitive inhibitors usually resemble the __ in structure

A

substrate

530
Q

Competitive inhibitors can be overcome with

A

high substrate/inhibitor ratios

531
Q

Noncompetitive inhibitors bind to

A

sites other than active sites and inactivate the enzyme

532
Q

With noncompetitive inhibitors the maximum velocity of enzyme molecules

A

can’t be reached

533
Q

T or F? Noncompetitive enzymes can be overcome with high substrate/inhibitor ratios

A

F

534
Q

Competitive inhibition increases K(m) without affecting

A

V(max)

535
Q

Noncompetitive inhibition reduces V(max) without affecting

A

K(m)

536
Q

Coupling by a scaffold protein overcomes

A

slow substrate diffusion in a metabolic pathway

537
Q

Describe the sequential action enzymes by which reaction pathways convert substrate into final products

A
  • enzymes free in solution: reaction intermediates diffuse from one enzyme to the next, which may be inherently slow
  • multisubunit enzyme complex formed by a scaffold protein minimizes or eliminates substrate diffusion time
  • some enzymes are fused at the genetic level, becoming domains in a single polypeptide chain-also minimizes or eliminates substrate diffusion time
538
Q

Proteins may be regulated at the level of

A
  • protein synthesis (transcription/translation)
  • protein degradation
  • through non covalent or covalent interactions
539
Q

Proteins marked for destruction with a polyubiquitin tag by ubiquitin ligases are degraded in

A

proteasomes

540
Q

Several allosteric mechanisms act as switches, reversibly turning __ on and off

A

protein activity

541
Q

Higher-order regulation includes

A

the intracellular compartmentation of proteins (sub cellular localization)

542
Q

What is covalent modification of a protein?

A

a molecule is covalently attached to the protein, thereby changing its chemical composition and altering the 3D structure of the protein

543
Q

What are examples of covalent modification?

A
  • phosphorylation
  • glycosylation
  • ubiquitination
544
Q

What is allosteric modification of a protein?

A

a molecule non-covalently interacts with the protein, thereby producing modest changes in the 3D conformation of the protein, resulting in a change in activity or interaction with other macromolecules

545
Q

What are some examples of allosteric modification?

A

interaction with metal co-factors or nucleotide

546
Q

What are post-translational modifications (PTMs)?

A

alterations to the side chains of the amino acids after their incorporation into a polypeptide chain

547
Q

Post-translational modifications (PTMs) can occur in

A
  • the cytoplasm
  • golgi apparatus
  • endoplasmic reticulum
548
Q

Post-translational modifications (PTMs) allow a single polypeptide to exist as

A

a number of distinct biological molecules

549
Q

What are three common forms of PTMs?

A
  • phosphorylation
  • glycosylation
  • ubiquitination
550
Q

PTMs are specific to

A

different amino acids

551
Q

In phosphorylation-dephosphorylation regulation of protein activity, kinases

A

transfer terminal phosphate group from ATP to specific Serine/Threonie or Tyrosine OH groups

552
Q

In phosphorylation-dephosphorylation regulation of protein activity, phosphatases

A

hydrolyze phosphate group off protein

553
Q

Kinases and phosphates work in pairs to regulate

A

protein activity

554
Q

Enzymes can be regulated by phosphorylation/dephosphorylation by

A

having the covalent modification alter the shape of the enzyme to regulate substrate-binding specificity

555
Q

Transcription factors can be regulated by phosphorylation/dephosphorylation by

A

having the covalent modification alter the shape of the protein to regulate sub cellular localization

556
Q

Protein degradation regulates

A

life spans of intracellular proteins- vary from as short as a few minutes for mitotic cyclins to as long as the age of an organism for proteins in the lends of the eye

557
Q

Protein degradation removes

A

damaged proteins

558
Q

The proteasome molecular machine

A

degrades targeted proteins

559
Q

What is polyubiquitinylation?

A

the addition of a polymeric chain of ubiquitins, usually marks protein for degradation

560
Q

What is monoubiquitinylation?

A

attachment of a single ubiquitin to a protein, alters protein function or sub cellular localization

561
Q

What is multiubiquitinylation?

A

addition of multiple, single ubiquitins; alters protein function or sub cellular localization

562
Q

Non-covalent binding of regulatory molecule to allosteric site

A

changes the conformation of a protein

563
Q

Allosteric switches control

A

protein activity

564
Q

What is Calmodulin?

A

a widely distributed cytosolic protein; contains four EF hand Ca2+ binding sites
-(helix-loop-helix motif; Kd of 10^-6 M)

565
Q

GTPase superfamily proteins exist in two forms/conformation, what are they?

A

GTP-bound and GDP-bound

566
Q

GTPases hydrolyze __ to __

A

GTP; GDP

567
Q

What is the conformation of the GTP-bound form of GTPase?

A

active “on” conformation

568
Q

The GTP-bound form of GTPase can

A

interact with target proteins to regulate their activities

569
Q

What is the conformation of the GDP-bound form of GTPase?

A

inactive “off” conformation

570
Q

What does guanine nucleotide exchange factor (GEF) do?

A

stimulates replacement (exchange) of the bound GDP (off) with a GTP (on)

571
Q

What does GTPase-activating protein (GAP) do?

A

stimulates GTP (on) hydrolysis to GDP (off)

572
Q

What are the four basic molecular genetic processes?

A
  1. transcription
  2. RNA processing
  3. translation
  4. DNA replication
573
Q

What happens in transcription?

A

the four-base DNA code specifying the amino acid sequence of a protein is copied (transcribed) into a precursor messenger RNA (pre-mRNA) by the polymerization of ribonucleoside triphosphate monomers (rNTPs)

574
Q

What happens in RNA processing?

A

removal of noncoding sequences and other modification to pre-mRNA to make mRNA, which is transported to the cytoplasm

575
Q

What happens in translation?

A

in ribosomes, tRNAs base pair with mRNA codons to position specific amino acids where they are linked into proteins

576
Q

What happens in DNA replication?

A

OCCURS ONLY IN CELLS PREPARING TO DIVIDE; deoxyribonucleoside triphosphate monomers (dNTPs) are polymerized to yield two identical copies of each chromosomal DNA molecule, one for each daughter cell

577
Q

DNA replication only occurs in cells

A

preparing to divide

578
Q

In DNA, two phosphoester bonds (phosphodiester bond) link

A

adjacent nucleotides

579
Q

Polynucleotides are synthesized in the __ to __ direction

A

5’ to 3’ (left to right)

580
Q

In the DNA double-helical structure, there are __ percentages of A=T and G=C

A

equal

581
Q

Interaction with a protein can __ DNA

A

bend

582
Q

The conserved C-terminal domain of the TATA box- binds to

A

the minor groove of specific DNA sequences rich in A and T

-this untwists and sharply bends the double helix

583
Q

Transcription of most eukaryotic genes requires participation of

A

TBP

584
Q

Which is more stable, DNA or RNA?

A

DNA

585
Q

Because DNA is more stable than RNA, it is a better carrier of

A

genetic information

586
Q

Why is RNA less stable than DNA?

A

because the 2’ hydroxyl group in RNA (absent in DNA) can act as a nucleophile, attacking the phosphodiester bond and breaking the strand

587
Q

The G/C content of DNA affects

A

melting temp

588
Q

DNA strands unwind and separate during replication and transcription by

A

breaking the hydrogen bonds between base-paired bases

589
Q

DNA denaturation/melting can be induced experimentally by

A

raising temp

590
Q

What is T(m)?

A

“temp of melting”; temp at which half the double-stranded DNA bases have melted/denatured

591
Q

The greater the G+C percentage, the higher the

A

T(m)

592
Q

What are some characteristics of RNA?

A
  • has a hydroxyl at 2’
  • uracil base instead of thymine
  • usually single-stranded
593
Q

Ribozyme RNAs have catalytic activity based on

A

tertiary structures formed by base pairing

594
Q

Base pairing between distant complementary segments of an RNA molecule forms

A
  • hairpins (5-10 nucleotide loop
  • stem-loops (11-100s of nucleotide loop)
  • other structures including pseudo knots that contribute to tertiary structure
595
Q

RNA is synthesized

A

5’ –> 3’

596
Q

One gene DNA strand is template for __ by pairing complementary bases

A

transcription of an RNA

597
Q

RNA polymerase begins transcription at gene nucleotide designated

A

+1

598
Q

The RNA polymerase travels “downstream” toward the __ end on the DNA, and downstream bases are designated with __ numbers

A

3’; positive

599
Q

“Upstream” bases are designated with __ numbers

A

negative

600
Q

What important gene features lie upstream of the transcription start site?

A

promoting sequences recognized by transcription factors that recruit RNA polymerase to the gene

601
Q

DNA strand being transcribed is the __

A

template strand

602
Q

The complement to the template strand is the

A

nontemplate strand

603
Q

RNA synthesized is complementary to the __ strand and is therefore identical with the nontemplate strand sequence, except with uracil in place of thymine

A

template

604
Q

Regulation of eukaryotic gene transcription is __ compared to regulation in prokaryotes

A

much more complex

605
Q

The promoter region of eukaryotic genes contain

A

enhancers

606
Q

What are enhancers?

A

short DNA sequence motifs to which specific transcription factors bind to recruit the molecular machinery necessary to transcribe mRNA

607
Q

What is combinatorial control?

A

eukaryotic gene regulation is in response to many integrated signals, activating numerous transcriptional regulators that converge on multiple enhancers within a single gene to differentially regulate activation or repression of gene expression

608
Q

What are the 3 stages of transcription?

A

initiation, elongation, termination

609
Q

What is initiation of transcription?

A

RNA polymerase melts DNA duplex to form a transcription bubble and begin polymerizing ribonucleotides (rNTPs) at the start site

610
Q

What happens during elongation in transcription?

A

polymerase advances 3’-5’ down template strand polymerizing one rNTP at a time onto the 3’ end of growing RNA. The 5’ end of the RNA strand is displaces from the template DNA and exits through a channel in the RNA polymerase

611
Q

What happens during termination in transcription?

A

RNA polymerase dissociates from the template DNA at a specific termination sequence (stop site)

612
Q

Initial transcript in eukaryotes is referred to as the

A

precursor or pre-mRNA

613
Q

What is RNA processing?

A

when several modifications must occur to generate a mature mRNA that can be exported to the cytoplasm for translation

614
Q

RNA processing produces __ __ in eukaryotes

A

functional mRNA

615
Q

RNA polymerase starts transcription at __ , which is upstream of the codon that encodes the first amino acid

A

gene nucleotide +1

616
Q

Where does RNA polymerase stop transcription?

A

downstream of the translation STOP codon

617
Q

The 5’ and 3’ unsaturated regions (UTRs) are __ in the fully processed mRNA

A

retained

618
Q

What is capping?

A

when specific enzymes add an atypical molecule (a guanosine methylated on its nitrogenous base (7-methylguanosine) attached in a 5’ 5o 5’ manner) to the 5’ end of transcript

619
Q

When does capping occur?

A

shortly after transcription begins during formation of the primary transcript

620
Q

What does capping do?

A
  • facilitates nuclear export
  • protects mRNA from degradation
  • promotes translation
  • promotes intron splicing
621
Q

What is polyadenylation?

A

when transcription is completed enzymes cleave the 3’ end of the transcript at a specific sequence (the polyadenylation sequence AAUAAA) and adds a string of adenine nucleotides- 150-200 adenine

622
Q

What does the poly(A) tail do?

A
  • stabilizes mRNAs in the nucleus and cytoplasm

- promotes mRNA translation

623
Q

Poly-A tails become shorter over time leading to

A

decreased translation

624
Q

What does splicing do?

A

removes introns and joins exons

625
Q

Splicing is initiated while

A

mRNAs are still being transcribed

626
Q

Conserved sequences __ , and are essential for their removal

A

define the 5’ and 3’ boundaries of exons/introns

627
Q

What is the donor site of RNA processing?

A

5’ end of intron

628
Q

What is the acceptor site of RNA processing?

A

3’ end of intron

629
Q

Many eukaryotic transcripts are

A

alternatively spliced

  • cell-type specific splicing
  • in response to external stimuli
  • at different stages of development
630
Q

Alternative splicing produces distinct proteins that lack/possess unique functional domains, and therefore

A

behave differently from one another

631
Q

Alternative RNA splicing

A

increases the number of protein isoforms expressed from a single eukaryotic gene

632
Q

What are the 3 RNAs involved in protein synthesis?

A

mRNA, tRNA, and rRNA

633
Q

What does mRNA?

A

nucleotide sequence that encodes the order of amino acids a ribosome assembles into polypeptide chain

634
Q

Each amino acid is encoded by a __ within the mRNA sequence

A

three-nucleotide codon

635
Q

Each amino acid is covalently bound to a subset of tRNAs containing a specific

A

three-nucleotide anticodon sequence

636
Q

Ribosomes are composed of numerous proteins and three (bacterial) or four (eukaryotic)

A

ribosomal RNA (rRNA) molecules

637
Q

One of the rRNAs

A

catalyzes peptide bond formation between incoming aa-tRNA amino-group and the carboxyl-terminus of the growing protein chain

638
Q

What happens in translation?

A

sequences of nucleotides in an mRNA direct the incorporation of 20 specific amino acids in a polypeptide

639
Q

What is the genetic code?

A

the set of rules by which the translation machinery reads the info in mRNAs and translates it into amino acid sequence

640
Q

What is a codon?

A

mRNA sequences are real as a series of three nucleotide “words”: each corresponding to a specific amino acid

641
Q

__ possible combos of triplet codons can be generated by the 4 nucleotides (U,C,A,G)

A

64

642
Q

The codons encoding one amino acid may differ in

A

any of their three positions (most often this difference is in the second or third position)

643
Q

No codon specifies more than one

A

amino acid

644
Q

An mRNA molecule can be read/translated in any of the three different reading frames:

A

-dividing the sequence of nucleotides in the mRNA into three-nucleotide codons- only 1 of the 3 reading frames specifies the correct protein

645
Q

Initiating translation in the incorrect frame can

A

produce a non-functional protein that may have deleterious effect on the cell

646
Q

T or F? Codons bind directly to their complementary amino acid

A

F

647
Q

Translation requires adaptor molecule, __, that bind the codon on one end and deliver an amino acid, bound at the other end, to the ribosome

A

transfer RNAs (tRNAs)

648
Q

tRNAs adopt a cloverleaf shape through

A

complementary intramolecular base-pairing

-this creates 4 double helical arms in each molecule

649
Q

The D loop of tRNA is important for

A

recognizing the enzyme that attaches the amino acid to each tRNA

650
Q

The T loop of tRNA is important for

A

recognizing the ribosome

651
Q

Each tRNA contains a specific anticodon that base pairs to codons in

A

the mRNA

652
Q

The first nucleotide of the anticodon (5’ end) pairs with the third nucleotide (3’ end) of the

A

codon

653
Q

Some anticodons can pair with more than one codon due to a phenomenon known as

A

wobble base pairing

654
Q

The significance of wobble base pairing effect is that

A

instead of 64 different tRNAs (one for each codon), organisms can have significantly fewer (min 31)

655
Q

Humans have __ tRNA genes, that encode __ distinct tRNAs

A

500; 48

656
Q

What are aminoacyl-tRNA synthetases?

A

specific enzymes that catalyze the covalent attachment of the appropriate amino acid to each tRNA

657
Q

What is the acceptor stem of tRNA?

A

a conserved CCA sequence in the 3’ end of tRNA where the appropriate amino acid will be covalently attached via its C-terminus

658
Q

Once an amino acid is attached, the tRNA is said to be

A

charged or activated

659
Q

Each aminoacyl-tRNA synthetase has

A
  • a docking site for tRNAs
  • a recognition site for the anticodon
  • a catalytic site for transferring the amino acid to the acceptor stem
660
Q

Covalent attachment of the amino acid is

A

ATP dependent and produces a high energy ester bond (unstable bond)

661
Q

What are ribosomes?

A

complexes composed of enzymatic ribosomal RNA (rRNA) and numerous accessory proteins

662
Q

What do ribosomes do?

A
  • move along a mRNA (5’ to 3’)
  • read each codon
  • accept the appropriate tRNA and
  • catalyze the covalent attachment of the next amino acid in the growing polypeptide chain
663
Q

Ribosomes share structural and functional similarities, but differ in

A

number of rRNAs and proteins in bacteria, archaea, and eukaryote

664
Q

What is the large ribosomal subunit of ribosomes composed of?

A

3 distinct rRNA molecules and many accessory proteins

665
Q

What is the small ribosomal subunit of ribosomes composed of?

A

a single rRNA molecule and many accessory proteins

666
Q

What does the small ribosomal subunit of ribosomes do?

A

matches tRNAs to mRNA codons

667
Q

What does the large ribosomal subunit of ribosomes do?

A

catalyzes formation of peptide bonds between new amino acid and the growing polypeptide

668
Q

LSU and SSU join together on the 5’ end of an mRNA to

A

initiate translation

669
Q

Ribosomes move in a __ direction along the mRNA synthesizing the polypeptide beginning with its __ terminus

A

3’ to 5’; N

670
Q

An assembled ribosome contains 3 binding sites for tRNAs that coordinate the processive covalent attachment of amino acids:

A

A, P, and E sites

671
Q

Amino acids are polymerized as they remain

A

attached to a tRNA

672
Q

__ make up the bulk of the ribosomal subunits

A

rRNAs

673
Q

rRNAs form the __ as well as the __ in the LSU

A

A, P, and E sites; catalytic transferase site

674
Q

Ribosomal proteins are primarily

A

structural

675
Q

SSU is bound by proteins collectively called __ and the __ in the P site

A
  • translation initiation factors

- initiator tRNA

676
Q

Initiator tRNAs provide the __ for the encoded peptide

A

first amino acid

677
Q

What does AUG do?

A
  • serves as the principle start codon

- encodes the amino acid methionine

678
Q

Only an __ can deliver the first amino acid.

A

initiator tRNA

679
Q

With the initiator tRNA in the P site and paired with the start codon,

A

the initiation factors disassociate, and the LSU complexes with the SSU
-Translation may now proceed

680
Q

When does elongation begin?

A

A charged/activated tRNA with anticodon complementary to the next codon enters the A site

681
Q

What is the first step of translation?

A

-the growing polypeptide remains covalently linked to the tRNA that just delivered the third amino acid.
-this tRNA and peptide is positioned in the P site (peptidyl) and remains base paired with the codon for that amino acid
-a charged tRNA enters the A-site and
base pairs with the codon specifying the
next amino acid.

682
Q

What is the second step of translation?

A
  • the LSU catalyzes covalent linkage of the polypeptide chain to the new amino acid
  • the C-terminus of the polypeptide is covalently joined to the N-terminus of the new amino acid
  • the polypeptide is transferred from the tRNA in the P site to the tRNA in the A site.
683
Q

What is the third step of translation?

A
  • the LSU translocates toward the 3’ end of the mRNA, shifting the two tRNAs from P-A to E-P in the LSU
  • the E site (empty) holds the recently depleted tRNA
  • the P site now holds the tRNA with the growing polypeptide
684
Q

What is the fourth step of translation?

A
  • the SSU translocates toward the 3’ end of the mRNA, bringing it back into its original position with the LSU
  • this causes the empty tRNA to be ejected from the E site
  • P site holds the peptide tRNA
  • the A site now contains the next codon to be be processed
685
Q

When is prokaryote and eukaryote translation terminated?

A

when a ribosome encounters one of three stop codons – UAA, UAG, UGA

686
Q

What are release factors (eRF3-GTP), and what do they do?

A

proteins that bind stop codons in the A site – altering catalytic activity of the LSU peptide transferase
-this adds a water molecule, rather than another amino acid, to the C-terminus of the peptide – freeing the polypeptide

687
Q

Circular mRNA, polysomes, and rapid ribosome recycling

A

increase the efficiency of translation

688
Q

Association of three proteins – poly(A)-binding protein (PABP), eIF4E, and eIF4G

A

circularizes mRNA by forming a bridge between the 5′ (cap) and 3′ (poly A) ends of the mRNA

689
Q

What is a polyribosome?

A

structure with multiple individual ribosomes simultaneously translating a eukaryotic mRNA