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MCAT BIO > BIO 1 > Flashcards

BIO 1 Flashcards

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1
Q

Reaction that links monomers

A

Dehydration synthesis

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2
Q

Opposite of dehydration synthesis

A

Hydrolysis

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3
Q

The only AA with no chiral carbon

A

glycine

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4
Q

Amphoteric

A

Can act as acid or base

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5
Q

Amphipathic

A

molecule has polar and nonpolar regions

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6
Q

Zwitterion

A

The amine group is protonated to NH3+, the carboxyl group deprotonated to COO-
(Form of AA at the isoelectric point pI)

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7
Q

Acidic AAs

A

Aspartic acid, Glutamic acid

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8
Q

Basic AAs

A

Lysine, Arginine

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9
Q

AA residues are (pos/neg) charged at physio pH

A

Negative

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10
Q

Basic amino acid residues are (pos/neg) charged at physio pH

A

Positive

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11
Q

AA residues that are positively charged at physio pH

A

Lysine, Arginine, Histidine

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12
Q

pI

A

Isoelectric point - pH at which molecule has 0 net charge

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13
Q

When pH is lower than the pI of the AA, the AA will be net (pos/neg) charged

A

Positive (protonated)

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14
Q

When pH is higher than the pI of the AA, the AA will be net (pos/neg) charged

A

Negative (deprotonated)

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15
Q

When pH < pI, the (pos/neg) charge version of the AA will predominate

A

Positive (protonated)

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16
Q

When pH > pI, the (pos/neg) charge version of the AA will predominate

A

Negative (deprotonated)

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17
Q

Do peptide bonds rotate

A

No because one of the resonance forms is a double bond between C=N

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18
Q

Primary structure, bond types

A

Sequence of AAs - peptide bond

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19
Q

Sequence of AAs written

A

N –> C

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20
Q

Secondary structure, bond types

A

Alpha helices, beta sheets - hydrogen bonds (in protein scaffold, not R groups)

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21
Q

Tertiary structure, bond types

A

Noncovalent between R groups (polar interactions, nonpolar interactions, electrostatic/acid/base)

Disulfide bridges

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22
Q

Quaternary structure

A

Interactions between multiple polypeptides

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23
Q

General formula for monosaccharides

A

C(n)H(2n)O(n)

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24
Q

General formula for disaccharides

A

C(n)H(2n-2)O(n-1)

one water molecule was lost - dehydration synthesis

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25
Q

Three common hexoses

A

Glucose, Fructose, Galactose (C6H12O6)

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26
Q

Two common pentoses (C5H10O5)

A

Ribose (C5H10O5), Deoxyribose (C5H10O4)

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27
Q

Glucose + Glucose = ? and bond type

A

Maltose, alpha bond

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28
Q

Glucose + Fructose = ? and bond type

A

Sucrose, alpha bond

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29
Q

Glucose + Galactose = ? and bond type

A

Lactose, beta bond

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30
Q

Three types of polysaccharides and their bond types

A

Glycogen (alpha-linked glucose), Starch (alpha-linked glucose), Cellulose (beta-linked glucose)

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31
Q

Fatty acid structure

A

Carboxylic acid head, hydrocarbon tail (saturated or unsaturated)

32
Q

(Saturated/Unsaturated) fats are (solid/liquid) at room temp

A

Saturated - solid at RT

Unsaturated - liquid at RT

33
Q

Triglyceride structure

A

1 Glycerol molecule + 3 fatty acids

34
Q

Triglyceride structure

A

1 Glycerol + 3 fatty acids

35
Q

Phospholipid structure

A

1 Glycerol + 2 fatty acids + 1 phosphate

36
Q

(Triglycerides/Phospholipids) are amphipathic

A

Phospholipids

37
Q

What is the monomer of terpenes

A

Isoprene

38
Q

Structure of isoprene

A

C5H10 (see pic)

39
Q

An example of a (tri)terpene

A

Squalene

40
Q

How many isoprenes = 1 terpene

A

2 (at least)

41
Q

Cholesterol (and derivatives) structure description

A

three 6-membered rings, one 5-membered ring

42
Q

Gibb’s free energy equation

A

dG = dH - TdS

43
Q

Terms for energy entering system vs energy leaving system

A

Endergonic; exergonic

44
Q

Sign of dG for a spontaneous reaction

A

negative

45
Q

Sign of dH for exothermic reaction

A

negative

46
Q

Sign of dH for endothermic reaction

A

positive

47
Q

Sign of dS for increasing disorder

A

positive

48
Q

Sign of dS for increasing disorder

A

positive

49
Q

Reaction often coupled to unfavorable reactions to make them proceed

A

ATP hydrolysis:

ATP –> ADP + Pi

50
Q

Reaction speed depends on ____

A

Stability of the transition state

51
Q

Ea

A

Activation energy needed to achieve transition state

52
Q

How do catalysts speed up reactions

A

They lower Ea by stabilizing the transition state of the reaction

53
Q

Ribozymes

A

enzymes made of RNA

54
Q

Allosteric site

A

Regulates enzyme activity (can open/close the active site) depending on what binds in allosteric site

55
Q

Negative feedback in an enzyme cascade

A

Accumulation of product causes inhibition of the enzyme that makes that product, or something upstream

56
Q

Positive feedback in an enzyme cascade

A

A –> B –> C –> D
Accumulation of product C causes upregulation of enzyme that catalyzes B–>C, because substrate B is toxic at high levels

57
Q

Draw graph of velocity vs substrate concentration, label Km, Vmax, and relative concentrations of substrate vs enzyme at different points on the graph

A

See pic

58
Q

Vmax depends mostly on _____

A

enzyme concentration (if you ever see Vmax changing, [E] is changing)

59
Q

Km

A

The substrate concentration [S] needed to reach 1/2 Vmax

60
Q

Increasing Km means (increasing/decreasing) enzyme affinity

A

Decreasing

61
Q

(Direct/Inverse) relationship between Km and enzyme affinity

A

Inverse

62
Q

Three types of enzyme inhibition

A

Competitive, Noncompetitive, Uncompetitive

63
Q

Competitive inhibitor: Where it binds, effect on Vmax, effect on Km

A

Binds at active site
No effect on Vmax
Increases Km

64
Q

Noncompetitive inhibitor: Where it binds, effect on Vmax, effect on Km

A

Binds at allosteric site
Decreases Vmax
No effect on Km

65
Q

Uncompetitive inhibitor: Where it binds, effect on Vmax, effect on Km

A

Binds at allosteric site of ES complex
Decreases Vmax
Decreases Km

66
Q

The only inhibition type that does not change Vmax

A

Competitive

67
Q

Type of inhibition where effectively fewer enzyme molecules are available to bind, but the enzyme affinity is still the same

A

Noncompetitive

68
Q

Type of inhibition that increases the observed enzyme affinity by making it harder for the ES complex to let go of its product

A

Uncompetitive

69
Q

Mixed inhibitor: where it binds, effect on Vmax, effect on Km

A

Binds at allosteric site or ES complex
Decreases Vmax
Km: depends
- If inhibitor has higher affinity for ES complex, then it acts as uncompetitive and Km decreases
- if inhibitor has higher affinity for the enzyme by itself, then it acts as competitive and Km increases
- if inhibitor has equal affinity for E and ES, Km does not change

70
Q

Lineweaver Burk plot: axes

A

x axis: 1/[S]

y axis: 1/V

71
Q

Lineweaver Burk plot: y-intercept

A

1/Vmax

72
Q

Lineweaver Burl plot: x-intercept

A

-1/Km

73
Q

LB plot for competitive inhibition (vs uninhibited)

A

Competitive inhibition:

  • Slope is steeper
  • x-intercept is closer to the origin
  • Same y-intercept
74
Q

LB plot for noncompetitive inhibition (vs uninhibited)

A

Noncompetitive inhibition:

  • Slope is steeper
  • Same x-intercept
  • y-intercept is farther from origin
75
Q

LB plot for uncompetitive inhibition (vs uninhibited)

A

Uncompetitive inhibition:

  • Same slope
  • x-intercept is farther from origin
  • y-intercept is farther from origin
76
Q

The only inhibitor type that does not change the slope of the LB plot

A

Uncompetitive

MCAT BIO (3 decks)

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