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egzam 1 cb Flashcards

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Biology 101 flashcards
1
Q

Polymers of polysaccharides, fats, and proteins are all synthesized from monomers by

A

CONDENSATION/dehydration Reaction (removing H2O)

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2
Q

Mitochondria was likely a _____ bacteria that got engulfed by a ______ cell.

A

aerobic; anaerobic

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3
Q

SNUD

A

saturated- no double bonds, unsaturated- double bonds

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4
Q

Smooth E.R

A

synthesizes fatty acids, phospholipids and cholesterol

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5
Q

Rough E.R

A

synthesizes proteins

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6
Q

Where are polysaccharides made?

A

Golgi Apparatus

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7
Q

How is carbon able to bond to 4 atoms?

A

by combining 2 orbitals (s & p)

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8
Q

All amino acids except ____ are Asymmetrical

A

Glycine

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9
Q

Mitochondria are present in all

A

Eukaryotes (plants and animals)

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10
Q

Cellular Respiration uses____ and produces ____

A

sugar; ATP

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11
Q

Whats the order they evolved in?

A

Anaerobic Prok
Anaerobic Euk
Photosynthetic Prok
Aerobic Prok
Aerobic Euk
Photosynthetic Euk

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12
Q

List the nonpolar forces

A

LDS, VW, D-D

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13
Q

Amino acids all have a ____ backbone

A

N-C-C

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14
Q

Glycosidic bonds link

A

a Sugar and a Sugar

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15
Q

A sugar linked to a base and a phosphate

A

Nucleotide

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16
Q

A sugar linked to a base

A

Nucleoside

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17
Q

The bond that links phosphate groups

A

phosphoanhydride bond

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18
Q

The bond that links 2 nucleotides

more specifically links the 3’ carbon atom of one SUGAR molecule and the 5’ carbon atom of another SUGAR

A

phosphodiester bond

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19
Q

The bond that links sugar and phosphate

A

phosphoester bond

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20
Q

From top to bottom list the parts of a phospholipid

A

hydrophilic (polar) head, Phosphate, Glycerol , hydrophobic fatty acid tail (non polar)

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21
Q

What is the greatest determinant whether the interaction between molecules will be transient or stable?

A

surface complementarity between molecules

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22
Q

What force/bond has the greatest impact on organization of lipid molecules with long hydrocarbon tails in the membrane?

A

hydrophobic forces

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23
Q

Once carbon has been turned to its most stable form, through what process can it return to its organic state?

A

photosynthesis

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24
Q

NADH and NADPH both carry two additional __________ and one additional __________.

A

2 electrons; 1 proton

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25
Q

How can you rank how oxidized molecules are?

A

The more O2 it has (less H+)

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26
Q

A positive +ΔG means the reaction is spontaneous or nonspontaneous?

A

Nonspontaneous

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27
Q

How do enzymes effect reactions?

A

they reduce the activation energy

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28
Q

True or false: Enzymes are not permanently altered by the reactions they catalyze

A

True

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29
Q

What is the DNA backbone made of?

A

sugar & phosphate

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30
Q

What 4 things are attached to the alpha carbon?

A
  1. a hydrogen
  2. an R group
  3. an amino group
  4. a carboxyl group
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31
Q

Only ___-amino acids are found in proteins

A

L

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32
Q

What are the two kinds of R-groups?

A
  1. Nonpolar/ hydrophobic
  2. Polar/ hydrophillic (can be CHARGED)
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33
Q

Uncharged yet polar amino acids tend to be found where?

A

On the surfaces of proteins

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34
Q

Acidic amino acids have what characteristic?

A

negative charge

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35
Q

Basic amino acids have what characteristic?

A

positive charge

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36
Q

True or false: Polypeptides have directionality

A

True

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37
Q

What is the amino group end of a polypeptide called?

A

N-terminus

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38
Q

What is the carboxyl group end of a polypeptide called?

A

C-terminus

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39
Q

What are the subunits of DNA and RNA called?

A

nucleotides

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40
Q

Base pairs are joined by what?

A

hydrogen bond

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41
Q

What are the 2 types of nucleic acids?

A

DNA and RNA

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42
Q

What kind of enzyme adds a phosphate group to another protein?

A

kinase

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43
Q

Purines include which 2 bases?

A

A & G

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44
Q

Pyrimidines include which 3 bases?

A

T & C & Uracil

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45
Q

What’s the difference between deoxyribose and ribose?

A

Deoxyribose lacks an Oxy on the 2′Carbon.

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46
Q

DNA backbones run in what direction

A

5’-3’ antiparallel

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47
Q

The nitrogenous bases are linked by what bonds?

A

hydrogen

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48
Q

The 3D shape of a molecule is influenced by ___________ interactions

A

intramolecular

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49
Q

The specific shape of the macromolecule is influenced by _______ bonds.
Whereas the shape of a protein is determined by _____________.

A

hydrophobic;
amino acid sequence

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50
Q

High levels of ____ are needed to complete chemical reactions

A

Heat

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51
Q

What is the sum of all the chemical reactions occurring in the cell?

A

Metabolism

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52
Q

What do catabolic reactions release?

A

energy

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53
Q

What is the 2nd Law of Thermodynamics?

A

Every energy transfer/transformation increases the entropy of the universe

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54
Q

What is the First Law of Thermodynamics?

A

Energy can not be created or destroyed

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55
Q

Photosynthesis equation

A

CO2 + H2O –> O2 + Sugar

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56
Q

Cellular Respiration equation

A

O2 + sugar –> CO2 + H2O

57
Q

True or False: In oxidation & reduction reactions 2 atoms do NOT form a polar covalent bond

A

False, a polar covalent bond occurs

58
Q

Adding hydrogen to a carbon atom is an example of what

A

reduction

59
Q

Removing hydrogen from a carbon atom is an example of what

A

oxidation

60
Q

Adding oxygen to a carbon atom is an example of what

A

oxidation

61
Q

Electrons are shifted away from the carbon, and the carbon atom becomes progressively more _______

A

oxidized

62
Q

What is Gibbs free energy?

A

Amount of energy in a system available to do work

63
Q

Y–> X
If the free energy of Y is greater than the free energy of X, is delta G positive or negative, and will the rxn occur spontaneously?

A

Reactants>product
would mean that there’ll be excess energy released. Exergonic rxns release energy. The delta G would be negative and hence the rxn is spontaneous. (this is favorable)

64
Q

X–> Y
If the free energy of Y is greater than the free energy of X, is delta G positive or negative, and will the rxn occur spontaneously?

A

Product>Reactant
would mean that there’ll be energy consumed. Endergonic rxns use energy. The delta G would be positive and hence the rxn is nonspontaneous.

65
Q

Enzymes reduce the energy needed to initiate (spontaneous or nonspontaneous?) reactions

A

spontaneous

66
Q

What do enzymes do during a chemical reaction?

A

stabilize the transition state (the high energy intermediate) and lower the activation energy

67
Q

T/F: Enzymes help regulate metabolic pathways

A

T

68
Q

Energy released by energetically favorable reactions can be stored as chemical bond energy. What does the cell use to store this energy?

A

activated carriers (ex. ATP, NADH, NADPH)

69
Q

ATP supplies the energy for a cell to do work. Give one example of this

A

-Transport materials across membranes (pumps)
-Molecular motors

70
Q

The terminal phosphate of ATP can be readily transferred to other molecules. What is this process called?

A

phosphorylation

71
Q

In activation, ATp transfers a ____ to a molecule in order to produce a ________.

A

phosphate ; intermediate

72
Q

Removal of electrons from an atom is called

A

Oxidation

73
Q

Adding electrons to an atom is called

A

Reduction

74
Q

NADP+ is the ______ electron carrier. When it gains an H+ it becomes NADPH and is now the ______ agent for ______ reactions.

A

oxidized;
reducing agent; anabolic

75
Q

NADH is the ______ electron carrier. When it loses an H it becomes NAD+ and is now the ______ agent for _______ reactions.

A

reduced;
oxidizing agent; catabolic

76
Q

NAD+ is the _______ agent for ________ reactions.

A

oxidizing; catabolic

77
Q

NADPH is the ________ agent for _______ reactions.

A

reducing; anabolic

78
Q

Glycolysis is an example of what kind of reaction? Also is NAD+ involved?
(it’s the breaking down of glucose into 2 pyruvate)

A

catabolic; yes

79
Q

T/F !! Acetyl CoA is an activated carrier involved in metabolism !!

A

True, now repeat it

80
Q

Biotin is an example of a what?

A

activated carrier

81
Q

What does Biotin actively carry (aka transfer)?

A

the carboxyl group

82
Q

Condensation rxn vs Hydrolysis rxn: What’s the difference?

A

Condensation rxns JOIN together 2 things by removing an H2O
Hydrolysis rxns BREAK bonds by adding an H2O

83
Q

Where does the energy for the synthesis of macromolecules (polypeptides, polysaccharides, nucleic acids) come from typically?

A

the hydrolysis of nucleoside triphosphate

84
Q

During the synthesis of macromolecules, what else is made during the process?

A

a high energy intermediate

85
Q

How does a nuclei acid chain grow? Give steps

A

Start off with the existing DNA strand. A triphosphate nucleotide is added, but 2 phosphates are broken off to be used as energy. The nucleotide (still has a phosphate) attaches to the DNA strand.

86
Q

Polypeptide backbone

A

N-C-C

87
Q

The shape & function of a protein is specified by

A

its amino acid sequence

88
Q

What gives a protein its distinct and individual properties?

A

the R group

89
Q

What bonds hold polypeptides together?

A

Noncovalent (V.W, hydrogen bonds)

90
Q

Polypeptides fold into the conformation that has _____?

A

lowest energy

91
Q

In an aqueous environment, the polypeptide chain will fold to keep the _____ side chains on the inside and the _____ side chains on the outside.

A

nonpolar; polar

92
Q

Where in a protein can you find hydrogen bonds? (3 places)

A

backbone- backbone (btwn N-H “amino” & C-O “carboxyl”)
backbone - side chain
side chain - side chain

93
Q

Proteins fold into the conformation that has _______?

A

lowest energy

94
Q

If a protein is denatured by urea what will the protein do if urea is then removed?

A

return to its original shape

95
Q

What do Chaperone proteins do?

A

guide the folding of new polypeptides

96
Q

Some chaperone proteins can act as an isolation chambers. Explain this

A

the chaperone protein is like a container. It catches the newly formed polypeptide and puts it inside of itself allowing it to fold correctly. Once it does, the cap lifts and the protein is released.

97
Q

Primary structure

A

amino acid chain (polypeptide)

98
Q

Secondary Structure

A

Polypeptide gets folded into helices or pleated sheets

99
Q

Tertiary Structure

A

3D folding due to the side chain interactions

100
Q

Quaternary Structure

A

protein with at least 2 polypeptide chains

101
Q

Certain amino acids tend to form α helices while others dont. What’s one thing that can lead to destabilization of α helices?

A

the R group being too big or too small

102
Q

In proteins, α helices are almost always _______ (for some reason)

A

right-handed

103
Q

Transmembrane proteins have _________ic amino acid side chains.

A

hydrophobic

104
Q

α helices are found in transmembrane proteins such as receptor and transport proteins. oK? ok.

A

repeat it

105
Q

Why do α helices wrap around each other?

A

to minimize the exposure of hydrophobic side chains to the aqueous environment

106
Q

What causes the “pleat” of the β- pleated sheet?

A

side chains which point up and down

107
Q

How do Parallel vs Antiparallel β-sheets differ?

A

Parallel - the polypeptides are running in the same direction
Antiparallel- the polypeptides run in opposite directions

108
Q

Beta sheets occur due to _________ between the amine (NH) and carboxyl groups (CO) of the polypeptide backbone, thus making it very strong.

A

hydrogen bonds

109
Q

Amyloid structure is just stacked _________

A

β-sheets

110
Q

α-helices andβ-sheets make up around __% of a protein’s secondary structure

A

50%

111
Q

How are α-helices andβ-sheets connected?

A

looped regions that change the direction of the protein strand

112
Q

Chloroplasts have their own ____ & _____, just like mitocondria.

A

DNA & ribosomes

113
Q

Chloroplasts likely arose from ______ bacterium getting engulfed by a _______

A

photosynthetic; aerobic

114
Q

What is a protein domain?

A

a folded unit of the tertiary structure typically with a certain function

115
Q

T/F: Solvents dont break all noncovalent bonds

A

false

116
Q

A protein ______ is the modular unit from which many larger single-chain proteins are
constructed

A

domain

117
Q

Any substance that will bind to a protein is known as its ______.

A

ligand

118
Q

Enzymes bind the _______ (or inhibitors) at their active site. Active site is ON the enzyme!!

A

substrates

119
Q

The high-energy intermediate is called the _______

A

transition state

120
Q

If two species have the same amino acid sequences do the 2 different proteins serve the same function?

A

yes, since the structures are the same.

121
Q

Substrates bind to the ________ of an enzyme.

A

active site

122
Q

An allosteric inhibitor does what?

A

changes the shape of an enzyme-

123
Q

What is feedback inhibition?

A

when an enzyme’s activity is inhibited by its end product

124
Q

The architecture and function of a polysaccharide are determined by _____ and _____.

A

sugar monomers
positions of glycosidic linkages

125
Q

Hydrolysis of glycogen releases ______

A

glucose

126
Q

In aqueous solutions, many sugars form ______ through interactions btwn hydroxyl and carboxyl groups

A

rings

127
Q

Whats the most stable form of glucose

A

d-glucose

128
Q

The formation of a ring by d-glucose can result in two alternative forms.
These forms depend on the ________ of the _______ group on carbon number 1

A

orientation; hydroxyl

128
Q

The formation of a ring by d-glucose can result in two forms what are they?

A

α d-glucose (hydroxyl group downward)
β d-glucose (hydroxyl group upward)

128
Q

NADPH is involved in anabolic processes. Give one example of a anabolic reaction.

A

photosynthesis

129
Q

α-helices andβ-sheets are stabilized by what bonds?

A

hydrogen bonding

130
Q

_________ is a common way to regulate protein activity. Adding one will turn it on, and removing one will stop the activity.

A

phosphorylation

131
Q

2 polypeptides can be linked by ______ bonds.

A

disulfide

132
Q

cysteine and disulfide bonds are involved in ________ structure

A

tertiary

133
Q

What is Km and what does it tell us?

A

The substrate concentration at which enzymes work at half the max velocity. Km tells us how strongly a substrate is bound

134
Q

Antibodies are made of _________

A

4 polypeptides, 2 heavy chains & 2 light chains

135
Q

Vmax

A

the max rate of the enzymatic reaction. Is reached when the enzyme is saturated

136
Q

What bonds hold the light and heavy chains together?

A

disulfide

cell bio (2 decks)

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