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biochem > biochem1 > Flashcards

biochem1 Flashcards

1
Q

alpha carbon

A

one over from carbonyl

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2
Q

proteinogenic amino acids

A

encoded by human genetic code

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3
Q

achiral amino acid

A

glycine

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4
Q

L-amino acids

A

NH2 on the left in Fisher projection

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5
Q

all euk amino acids are

A

L-amino acids

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6
Q

all chiral amino acids are _____, except ______, which is ______

A

S, cysteine, R

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7
Q

amino acid whose amino nitrogen is part of the R group

A

proline

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8
Q

Nonpolar, nonaromatic

A

Leucine, isoleucine, methionine, proline, valine, alanine, glycine

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9
Q

Draw glycine

A

.

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10
Q

Draw alanine

A

.

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11
Q

Draw valine

A

.

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12
Q

Draw leucine

A

.

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13
Q

Draw isoleucine

A

.

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14
Q

Draw methionine

A

.

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15
Q

Draw proline

A

.

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16
Q

Aromatic polar

A

tyrosine (Y)

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17
Q

aromatic, non-polar

A

tryptophan (W), phenylalanine (F)

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18
Q

polar side chain amino acids

A 
GSTAC
glutamine (Q)
serine (S)
threonine (T)
asparagine (N)
cysteine (C)
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19
Q

abbreviation for glutamine

A

gln

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20
Q

abbreviation for glutamic acid

A

glu

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21
Q

negatively charged amino acids

A

aspartic acid (D) and glutamic acid (E)

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22
Q

positively charged amino acids

A

histidine, arginine, lysine (K)

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23
Q

hydrophobic amino acids

A

VIPLA

valine, isoleucine, proline, leucine, alanine

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24
Q

hydrophilic amino acids

A

acidic and basic

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25
Q

A

A

hydrophobic, alanine

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26
Q

R

A

positive charge, arginine

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27
Q

N

A

hydrophilic, asparagine

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28
Q

D

A

negative charge, aspartate

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29
Q

C

A

cysteine

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30
Q

E

A

negative charge, glutamate

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31
Q

Q

A

hydrophilic, glutamine

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32
Q

G

A

achiral, glycine

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33
Q

H

A

positive charge, histidine

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34
Q

I

A

hydrophobic, isoleucine

35
Q

L

A

hydrophobic, leucine

36
Q

K

A

positive charge, lysine

37
Q

M

A

methionine

38
Q

F

A

phenylalanine

39
Q

P

A

hydrophobic, proline

40
Q

S

A

serine

41
Q

T

A

threonine

42
Q

W

A

tryptophan

43
Q

Y

A

tyrosine

44
Q

V

A

hydrophobic, valine

45
Q

under acidic conditions, ionizable groups tend to ____ protons

A

gain

46
Q

under basic conditions, ionizable groups tend to ____ protons

A

lose

47
Q

at low PH, ionizable groups tend to be

A

protonated

48
Q

at high pH, ionizable groups tend to be

A

deprotonated

49
Q

pKa is the pH at which

A

[HA] = [A-]

50
Q

At a pH below the pKa,

A

majority of species is HA

51
Q

At a pH above the pKa,

A

majority of species is A-

52
Q

pKa1 refers to

A

carboxyl group (usually around 2)

53
Q

pKa2 refers to

A

amino group (around 9-10)

54
Q

at the isoelectric point,

A

every molecule is neutral

55
Q

formula for pI

A

pI = (pKa1 + pKa2)/2

56
Q

on a titration curve, things ____ protons on the way up

A

lose

57
Q

on a titration curve, things ______ protons on the way down

A

gain

58
Q

formula for pI of acidic amino acid

A

(pKa of R group + pKa of COOH group)/2

59
Q

formula for pI of basic amino acid

A

(pKa of amino group + pKa of R group)/2

60
Q

relatively low isoelectric points

A

acidic side chain

61
Q

acidic side chain

A

relatively low isoelectric point

62
Q

relatively high isoelectric point

A

basic side chain

63
Q

basic side chain

A

relatively low isoelectric point

64
Q

up to 20

A

oligopeptides

65
Q

oligopeptides

A

up to 20

66
Q

on the left

A

amino group

67
Q

peptide bond formation

A

removal of water, ie condensation or dehydration

68
Q

removal of water, ie condensation or dehydration

A

peptide bond formation

69
Q

peptide bond hydrolysis

A
  • add OH to carbonyl and H+ to amide nitrogen

- trypsins

70
Q
  • add OH to carbonyl and H+ to amide nitrogen

- trypsins

A

peptide bond hydrolysis

71
Q

primary structure

A

order of amino acids

72
Q

secondary structure

A

beta-pleated or alpha-helix

73
Q

beta-pleated and alpha-helix held together by

A

hydrogen bonds

74
Q

proline, as it relates to alpha helix and beta pleats

A

generally found in turns between beta sheets and at start of alpha helix, but not in the middle of either

75
Q

3D shape of protein

A

tertiary structure

76
Q

tertiary structure

A

3D shape of protein

77
Q

molten globule

A

intermediate form between secondary and tertiary structure

78
Q

denatured protein has lost

A

tertiary structure

79
Q

has lost tertiary structure

A

denatured protein

80
Q

why hydrophilic residues are found along the outside

A

water molecules have greater freedom in forming H-bonds, thus increasing entropy

81
Q

quarternary structure

A

structural unit composed of more than one polypeptide chain

82
Q

conjugated proteins

A

proteins with covalently attached molecules

83
Q

proteins with covalently attached molecules

A

conjugated proteins

84
Q

prosthetic groups may include

A

NICL vitamin

nucleic acid, metal ion, carbohydrate, lipid, vitamin

biochem (1 decks)

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