Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

DAT: Biology > Chapter 1 (Pt. 2) > Flashcards

Chapter 1 (Pt. 2) Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

what is a proteome?

A

all of the proteins expressed by a cell under certain conditions. like a genome for proteins.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

how can two different cells in the same organism have differing proteomes?

A

proteome is based on which genes are active in a cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is the subunit of polypeptides?

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what are polypeptides

A

polymers that make up proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what is the structure of an amino acid? (4)

A

central alpha carbon

amino group

carboxyl group

variable R group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

how many amino acids are there?

A

20 AAs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what happens to an AA at physiological pH?

A

amino group protonated, carboxyl group deprotonated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what is the value of physiological pH

A

7.4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is the role of peptide bonds?

A

attach AAs to each other

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

peptide bonds are formed by which type of reaction?

A

dehydration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

peptide bonds are broken by which type of reaction?

A

hydrolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what are the specific ends of a polypeptide?

A

C terminus (carboxyl)

N terminus (amino)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

describe primary protein structure.

what determines this?

A

sequence of AAs

genes.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

describe secondary protein structure.

what determines this?

A

local folds in a polypeptide chain.

H bonding between atoms on polypeptide backbone.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what is required for hydrogen bonding?

A

H binds to F, O, N

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

which parts of a protein will participate in hydrogen bonding?

A

carbonyl and amino groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what is tertiary protein structure.

what determines this?

A

3D folding pattern of the polypeptide.

due to R group interactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what are some R group interactions? (5)

A

ionic
hydrogen
dipole-dipole
london dispersion
hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what are disulfide bridges.

what is their role?

in what protein structure are they found?

A

covalent likages.

hold protein in most stable conf.

tertiary protein structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

folding of a tertiary protein structure positions nonpolar R groups where as a result of hydrophobic interaction?

A

inside a loop, isolated from water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

describe quaternary protein structure.

A

one large protein with multiple subunits.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

what does denaturing proteins mean?

what happens when proteins are denatured?

A

protein misfolding.

protein loses higher order structures, but primary structure is retained.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

name four common denaturation agents

A

heat
chemicals
pH changes
radiation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

protein misfolding causes what?

A

loss of shape –> loss of function

25
Q

what three principles govern catalysts

A
  • increase reaction rates
  • do not affect spontaneity
  • not used up in the reaction
26
Q

how do catalysts work?

A

lower activation energy

27
Q

what is the difference between an enzyme and a catalyst?

A

same rules apply, enzyme is a biological catalyst.

28
Q

what are enzymes made of?

A

proteins

29
Q

what is the active site made of?

A

AAs

30
Q

what does substrate specificity of an enzyme means?

A

enzyme only binds to certain molecules

31
Q

what is the enzyme specificity constant?

A

measure of an enzyme’s efficiency

32
Q

what does a high specificity constant mean? (2)

A
  • highly efficient enzyme
  • enzyme active site has a high substrate affinity
33
Q

what are the two enzyme models you learned in physiology?

A
  • lock and key model
  • induced fit theory
34
Q

induced theory states that…

A

enzymes slightly change shape to accomodate substrate

35
Q

lock and key model states that…

A

enzymes are rigid. not accurate.

36
Q

are all enzymes proteins?

A

no! ex. ribozymes (RNA)

37
Q

why would knowing about ribozymes be interesting?

A

they are an RNA enzyme, indicating that not all enzymes are proteins

38
Q

what are enzyme cofactors?

A

non-protein molecules that assist enzymes

39
Q

can you name the two types of enzyme cofactors with some examples of each?

A

i can.

  1. organic cofactors: vitamins (coenzymes; vitamin C)
  2. inorganic cofactors: metal ions (iron, potassium)
40
Q

what are holoenzymes/

A

enzyme bound to a cofactor

41
Q

what are prosthetic groups?

A

cofactors that bind covalently to their enzyme

42
Q

what would a holoenzyme look like in a nice little drawing?

A

it would be the one that has the cofactor or coenzyme bound to the enzyme

43
Q

what is an enzyme?

A

a biological catalyst. meaning, it increases reaction rates without affecting spontaneity or being used up in the reaction.

44
Q

what is an apoenzyme?

A

enzyme not bound to a cofactor.

45
Q

what would an apoenzyme look like in a nice little drawing?

A

the enzyme would not be bound to the cofactor/coenzyme

46
Q

what factors might affect enzymatic activity?

A

changes in pH/temp –> change shape –> change function

47
Q

what does “enzyme inhibition? mean?

A

interfering or suppressing normal enzyme function

48
Q

what is the difference between competitive vs. noncompetitive inhibition?

A

COMPETITIVE: inhibitors compete for active sites. adding substrate can overcome this type of inhibition.

NONCOMPETITIVE: inhibitor binds to allosteric site, which modifies active site. cannot be overcome by adding more substrate, because substrate and inhibitor don’t compete for active site.

49
Q

ENZYME KINETICS:

what is V?
what is Vmax?
what is [X]?

A

V: velocity. rate at which reaction occurs.

Vmax: maximum reaction velocity.

50
Q

how would Vmax be illustrated in a nice little drawing?

A

substrate has filled up all the enzymes.

51
Q

what the name of Km?

what does it represent?

A

Michaeli’s constant.

[X] at 50% of Vmax

52
Q

large Km = ?

why?

A

low affinity for substrate.

a lot of substrate was needed to get to 50% of Vmax

53
Q

small Km = ?

why?

A

high affinity for substrate

not a lot of substrate was needed to reach 50% of Vmax

54
Q

what happens to Vmax and Km under COMPETITIVE INHIBITION conditions?

A

Vmax stays the same

Km increases

55
Q

what happens to Vmax and Km under NONCOMPETITIVE INHIBITION conditions?

A

Vmax decreases

Km stays the same

56
Q

can you name three examples of enzymes?

A

sure i can! i learned about these in physiology.

phosphatase

phosphorylase

kinase

57
Q

what type of inhibition can be overcome by adding more substrate?

A

competitive

58
Q

what does a low Km imply as opposed to a high Km?

A

low: high affinity for X

high: low affinity for X

59
Q

how do enzymes increase reaction rate?

A

lowering the energy of the transition state, which lowers the activation energy

DAT: Biology (8 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions