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
h bond in alpha helix between
i and i+4
26
residues/turn for alpha helix
3.6
27
rise/residue for alpha helix
1.5 a
28
rise/turn for alpha helix
5.4
29
what aa in not common in alpha helix
proline
30
why are h bonds stronger in antiparallel
h bonds are strongest at 18- degrees
31
how many a between strands in bs
4
32
how many a between r groups on same bs face
7
33
which two aa are common in beta turns
proline and glycine
34
keratin coils are held together by
hydrophobic interactions
35
collegen is made up of
3 left hand helixes (gly-x-y, glycine proline hydroxyproline)
36
silk is
stacked antiparallel beta sheets
37
if u sub a hydrophobic aa for a hydrophilic aa would keratin form
no
38
pH
protein is positive (binds cation exchanger)
39
pH>pI in ion exchange
protein is negative (binds anion exchanger)
40
elution for ion exchange
increase salt to disrupt binding, adjust pH to change protein charge and reduce binding ability
41
diethylaminoethyl
weak anion exchanger
42
carboxymethyl
weak cation exchanger
43
which proteins elute first is sec
large
44
elution in affinity chromatography
high concentration of ligand solution
45
disfavorable entropy in protein folding
exteended chain to one folded conformation
46
favorable entropy change in pf
water molecules freeed
47
favorable enthalpy changes
stronger h-h bonds, salt bridges, dipole, and vdw
48
pI
point where net charge on protein is 0
49
lysine pkr
10.5
50
arginine pkr
12.5
51
histidine pkr
6
52
glutamic acid pkr
4
53
aspartate pkr
3.5
54
cysteine pkr
8
55
tyrosine pkr
10
56
carboxylic acid pkr
2-3
57
amine group pkr
8.5-9.5
58
hydrophobic aa
GAV LIMP
59
polar uncharged
stncq
60
basic aa
rkh
61
acidic aa
ed
62
aromatic aa
fwy