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BSCI170 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

Prokaryotes

A

unicellular
Eubacteria and Archaebacteria

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2
Q

Eukaryotes

A

some unicellular, mostly multicellular

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3
Q

Endomembrane System

A

nuclear envelope, endoplasmic reticulum, Golgi apparatus, lysosomes, endoscopes

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4
Q

Cytoplasm

A

everything between plasma and membrane and nuclear envelope

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5
Q

Cytosol

A

Gel-like substance excluding the membrane-bound organelles

includes the cytoskeleton and nonmembrane-bound inclusions

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6
Q

Organelles

A

discrete membrane-bound sub cellular compartments specialized to carry out specific cellular functions

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7
Q

Rough Endoplasmic Reticulum

A

lots of surface area and membrane, layers of flattened membrance studded with ribosomes for synthesis of protein

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8
Q

Smooth Endoplasmic Reticulum

A

no ribosomes, smooth tubules, cholesterol biosynthesis, membrane biosynthesis, detoxification

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9
Q

Golgi Apparatus

A

processes and packages material for secretion out of cell or to different part of the cell

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10
Q

Lysosomes

A

intracellular digestion…uses enzymes to digest/break down large materials such as fats, proteins, carbohydrates

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11
Q

Central Vacuole

A

stores water, ions, organic molecules, toxic metabolites

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12
Q

Mitochondrion

A

oxidation of carbohydrates and fatty acids and production of ATP

has its own ribosomes

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13
Q

Chloroplasts

A

photosynthesis and starch production

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14
Q

Cytoskeleton

A

series of proteinaceous filaments and tubules
controls cell shape, cell motility, replication, secretion, gene expression, etc

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15
Q

Microfilaments

A

Cytoskeleton
made up of strands of the protein actin, often interact with strands of other proteins

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16
Q

Intermediate filaments

A

Cytoskeleton
made up of fibrous proteins organized into tough, roselike assemblages that stabilize a cell’s structures and help maintain its shape

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17
Q

Microtubules

A

Cytoskeleton
long, hollow cylinders made u pof many molecules of the protein tubule

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18
Q

matter

A

anything that takes up space and has mass

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19
Q

compound

A

contains two or more different elements in a defined ratio

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20
Q

Trace elements

A

small but important

Fe in Heme
Iodine in Thyroid Hormone

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21
Q

smallest unit of structure containing all of the chemical and physical properties of an element

A

atom

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22
Q

strong and stable bond resulting from electron sharing

A

covalent bond

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23
Q

Molecule

A

two or more atoms held together by covalent bonds

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24
Q

measure of how strongly an atomic nucleus attracts and holds onto electrons

A

electronegativity

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25
Q

if a covalent bond is formed between two atoms of the same type, the electrons are shared equally

A

Nonpolar Covalent Bonds

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26
Q

unequal electron sharing

A

Polar Covalent Bond

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27
Q

Weak Bonds

A

hydrogen bonds, ionic bonds, van der Waals Interactions

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28
Q

when a Hydrogen covalently bonded to one electronegative atom is attracted to another nearby electronegative atom
weak bonds

A

Hydrogen bonds

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29
Q

electronegativity difference may be so large as to literally pull electrons from the outer shell
crystal

A

Ionic Bonds

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30
Q

molecules with nonpolar bonds can have localized regions of partial positive or partial negative charge

determine: 3D shape of proteins, interactions between enzyme and substrate, interactions of antigen-anitbody interactions

A

van der Waals Interactions

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31
Q

Properties of water

A

adhesion and cohesion
moderation of temperature (high specific heat)
heat of vaporization
evaporative cooling
solid H2O is less dense than liquid H2O

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32
Q

Plasma Membrane

A

the membrane found in all cells that separates the interior of the cell from the outside environment

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33
Q

Nucleus

A

stores DNA/genetic info

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34
Q

Nucleolus

A

The nucleolus is a spherical structure found in the cell’s nucleus whose primary function is to produce and assemble the cell’s ribosomes. The nucleolus is also where ribosomal RNA genes are transcribed.

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35
Q

What do chemical bonds result from

A

interactions between valence shell electrons between elements

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36
Q

Four different basic types of molecules

A

lipids, proteins, carbohydrates, nucleic acids

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37
Q

macromolecules

A

carbohydrates, proteins, lipids, and nucleic acids form huge molecules

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38
Q

monomer

A

subunits that make up macromolecules

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39
Q

polymer

A

chain of covalently attached monomers

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40
Q

dehydration synthesis

A

removes a water molecule, forming a new bond

one H2O released for every monomer added to the polymer

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41
Q

hydrolysis

A

one molecule of H2O added for every monomer removed from the polymer

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42
Q

saccharide

A

sugar

monosaccharide, polysaccharide, etc
monosaccharides have common structure

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43
Q

names that usually end in the suffix -ose

A

carbohydrates

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44
Q

covalent bond connecting monosaccharides

A

glycosidic linkage

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45
Q

functions of polysaccharides

A

energy storage
structure
protection
starch
glycogen

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46
Q

structural polysaccharides

A

polymers of ß-form monosaccharides
form rigid rods rather than loose helices
cellulose

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47
Q

cellulose

A

plant cell walls
most abundant organic molecule on Earth
dietary fiber

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48
Q

functions: energy storage, protection, recognition, and structural integrity

A

carbohydrates

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49
Q

Functions: energy storage, biomembrane structure, hormones

characterized by hydrophobicity

A

lipids

50
Q

No C=C

A

saturated

51
Q

One C=C

A

monounsaturated

52
Q

Many C=C

A

polyunsaturated

53
Q

why is water a universal solvent

A

hydrogen bonding

H2O forms a hydration shell, separating ions allowing them to dissolve in water

54
Q

increases the relative concentration of h+ in a solution

A

acid

55
Q

decreases the relative concentration of H+ in a solution

A

base

56
Q

why is carbon structurally loved in organic stuff

A

4 valence electrons, so it either needs 4 more or 4 less

forms single, double, or triple covalent bonds

57
Q

hydrocarbons

A

hydrogens and carbons
nonpolar covalent bonds
relatively unreactive

58
Q

molecules with the same molecular formulae but with distinct arrangements of the atoms

A

isomers

59
Q

specialized form of structural isomer where they differ in the arrangement of groups across a C=C

A

geometric isomers

cis = same side
trans = opposite side

60
Q

mirror image isomer molecules that differ in the orientation of atoms around an asymmetric carbon

A

enantiomers

61
Q

animal lipids

A

usually saturated fatty acids
tails pack tightly
solid at room temperature

62
Q

plant lipids

A

usually unsaturated fatty acids
tails pack more loosely
liquid at room temperature
oils

63
Q

phosphlipids

A

hydrocarbon chains
hydrophobic tail and hydrophilic head = amphipathic
bilayer segregates inside from outside

64
Q

steroids

A

4 fused carbon rings
hydrophobic

65
Q

Protein functions

A

Catalysts
structure
communication
transport
motility
defense
recognition
regulation
storage

66
Q

protein monomer

A

amino acid

67
Q

amino acid structure

A

amino group and carboxyl group
different R groups

68
Q

Polymer formation

A

amino group and carboxyl group are bonded with a peptide bond
dehydration synthesis –> water is released

69
Q

four levels of protein structure

A

primary, secondary, tertiary, quaternary

70
Q

protein structure that genetically determines linear sequence of amino acids

A

primary structure

71
Q

protein structure with hydrogen bonds within the backbone

A

secondary structure

72
Q

protein structure with molecular interactions between R groups within the chain

A

tertiary structure

73
Q

protein structure with subunit interactions

A

quaternary structure

74
Q

Spontaneous protein folding in Isolation

A

normal protein –> denaturation –> de natured protein –> renaturing (though not always)

75
Q

factors that impact final protein structure

A

temperature, ionic strength, pH

76
Q

correct protein folding

A

molecular chaperonin…fold molecules in teh right shape

77
Q

mutation that results from misfolded proteins

A

sickle cell disease anemia

78
Q

long, linear chains off covalently bonded nucleotide monomers
Function: storage and transmission of genetic informations

A

Nucleic Acids

79
Q

two types of nucleic acids

A

Ribonucleic Acid (RNA)
Deoxyribonucleic Acid (DNA)

80
Q

nucleic acid monomer

A

nucleotide
base + sugar

81
Q

Purines

A

Adenine and Guanine
RNA and DNA

82
Q

Pyrimidines

A

Cytosine (DNA and RNA)
Thymine (DNA)
Uracil (RNA)

83
Q

bond that joins nucleotides

A

phosphodiester bond

84
Q

Base pairing

A

A and T
G and C

85
Q

Metabolism

A

collection of all biochemical reactions occurring in a cell

86
Q

breakdown of larger, more complex molecules into smaller, less complex molecules

releases chemical energy

A

catabolism

87
Q

synthesis of larger, more complex molecules from smaller, less complex molecules

requires input of energy

A

anabolism

88
Q

Energy can be transferred and transformed but it cannot be created or destroyed

A

1st Law of Thermodynamics

89
Q

during every transformation, some energy becomes unusable to use –> heat

A

2nd Law of Thermodynamics

90
Q

unusable energy

A

entropy

91
Q

measure of disorder of the universe

A

entropy

92
Q

any process that occurs without input of energy

A

spontaneous

93
Q

energy available in a system to do work

A

free energy (G)

94
Q

total energy in a system

A

enthalpy

95
Q

∆G = ∆H - T∆S

A

amount of usable energy = total amount of energy - amount of usable energy

96
Q

spontaneous reaction

A

free energy is reduced
∆G is negative = exergonic

97
Q

∆G is negative

A

exergonic

98
Q

nonspontaneous reaction

A

free energy is increased
∆G is positive = endergonic

99
Q

∆G is postive

A

endergonic

100
Q

∆G is 0

A

equilibrium

101
Q

is all reactions are at equilibrium…

A

no free energy change –> no work –> dead cell

102
Q

anabolic reactions
building large molecules

A

chemical work

103
Q

directed movement
ciliary beating, muscle contration, chromosome separation

A

mechanical work

104
Q

building gradients
pumping substances across a membrane against a gradient

A

transport work

105
Q

generating light

A

bioluminescence

106
Q

what forms glycosidic linkage

A

dehydration synthesis

107
Q

what are nucleotides made of

A

nitrogenous base, 5C sugar, phosphate group

108
Q

What impacts optimal enzyme conditions?

A

temperature (optimal is 37 degrees C)
pH

109
Q

Saturation

A

rate of product formation is at a maximum
all functional enzyme molecules are binding substrate and converting it into product at MAX SPEED

110
Q

Enzyme effector molecules

A

Activators and Inhibitors

111
Q

Increase rate of product formation (in enzyme)

A

activators

112
Q

decrease rate of product formation (in enzyme)

A

inhibitors

113
Q

nonprotein enzyme activators

A

Cofactors

organic cofactor = coenzyme

114
Q

types of enzyme inhibitors

A

irreversible inhibitors and reversible inhibitors

115
Q

Covalent attachment to enzyme usually at active site

A

Irreversible inhibitors

116
Q

noncovalent attachment to enzyme

A

reversible enzyme inhibitors

117
Q

Types of reversible enzyme inhibitors

A

competitive and noncompetitive

118
Q

how can the effect of a competitive inhibitor be reduced

A

by increasing the concentration of substrate

119
Q

binds to enzyme away from active site
changing structure of enzyme, reducing ability of enzyme to function normally

A

noncompetitive inhibitor

120
Q

molecules that bind to an enzyme away from the active site

A

Allosteric regulatory molecules

121
Q

molecules that change the conformation and activity of the enzyme

A

regulatory molecules

122
Q

Conformations of multisubunit enzymes

A

functional and nonfunctional

BSCI170 (4 decks)

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