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BCH369 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

hydrophobic effect

A

increases entropy by freeing water molecules
number of unordered water molecules increases

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2
Q

peptide bond formation

A

dehydration/condensation, water removed

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3
Q

peptide bond breaking

A

hydrolysis, water is added

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4
Q

omega bond can either be ___ or ____ and is usually

A

180, 0, 180

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5
Q

which bond can rotate freely

A

phi and psi

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6
Q

phi

A

n - ca

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7
Q

psi

A

ca-c

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8
Q

which aa has more areas on rp

A

glycine

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9
Q

which aa has less areas on rp

A

proline

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10
Q

pka is what for protons

A

when pka=ph, 50% of protons are lost

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11
Q

what is the best buffering for a weak acid

A

+/- 1 ph from the pka

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12
Q

pka 1 for amino acids with neutral side chains

A

2

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13
Q

pka2 for amino acids with neutral side chains

A

9

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14
Q

if given a peptide with lots of rkh, what does this mean about pi

A

high pi

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15
Q

is pi is 2,3,4 what does this mean abt side chains

A

acidic side chains present

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16
Q

pi is the point where

A

the net charge on the protein is 0

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17
Q

at a pH below the pi

A

more protons available, side chains protonated, will have + charge

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18
Q

at pH above the pI

A

protons LEAVE, side chains are DEPROTONATED, there will be - charge

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19
Q

lower pI =

A

more acidic side chains (ED), easily deprotonated at physiological pH

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20
Q

higher pI

A

more basic side chains (RKH), harder to deprotonate at physiological pH

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21
Q

primary protein structure

A

linear arrangement of amino acids from n to c

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22
Q

secondary protein structure

A

regularly repearting pattern of H bonding from backbone chain

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23
Q

tertiary protein structure

A

many interactions between side chain to form 3d shape

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24
Q

quant protein structure

A

multiple tertiary structures associate w each other

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25
Q

h bond in alpha helix between

26
Q

residues/turn for alpha helix

27
Q

rise/residue for alpha helix

28
Q

rise/turn for alpha helix

29
Q

what aa in not common in alpha helix

30
Q

why are h bonds stronger in antiparallel

A

h bonds are strongest at 18- degrees

31
Q

how many a between strands in bs

32
Q

how many a between r groups on same bs face

33
Q

which two aa are common in beta turns

A

proline and glycine

34
Q

keratin coils are held together by

A

hydrophobic interactions

35
Q

collegen is made up of

A

3 left hand helixes (gly-x-y, glycine proline hydroxyproline)

36
Q

silk is

A

stacked antiparallel beta sheets

37
Q

if u sub a hydrophobic aa for a hydrophilic aa would keratin form

38
Q

pH<pI in ion exchange

A

protein is positive (binds cation exchanger)

39
Q

pH>pI in ion exchange

A

protein is negative (binds anion exchanger)

40
Q

elution for ion exchange

A

increase salt to disrupt binding, adjust pH to change protein charge and reduce binding ability

41
Q

diethylaminoethyl

A

weak anion exchanger

42
Q

carboxymethyl

A

weak cation exchanger

43
Q

which proteins elute first is sec

44
Q

elution in affinity chromatography

A

high concentration of ligand solution

45
Q

disfavorable entropy in protein folding

A

exteended chain to one folded conformation

46
Q

favorable entropy change in pf

A

water molecules freeed

47
Q

favorable enthalpy changes

A

stronger h-h bonds, salt bridges, dipole, and vdw

48
Q

pI

A

point where net charge on protein is 0

49
Q

lysine pkr

50
Q

arginine pkr

51
Q

histidine pkr

52
Q

glutamic acid pkr

53
Q

aspartate pkr

54
Q

cysteine pkr

55
Q

tyrosine pkr

56
Q

carboxylic acid pkr

57
Q

amine group pkr

58
Q

hydrophobic aa

59
Q

polar uncharged

60
Q

basic aa

61
Q

acidic aa

62
Q

aromatic aa

BCH369 (10 decks)

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