shit i actually will not remember lol Flashcards

1
Q

which AA is found at polar and non polar boundary

A

tryptophan

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2
Q

what is the functional group name in methionie

A

thiol ether

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3
Q

what does the average mass of aa value take into account

A

mass and frequency of incorporation

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4
Q

list the aromatic amino acids in order of decreasing polarity

A

histidine, tyrosine, tryptophan, phenylalanine

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5
Q

what wavelength do tyr and trp absorb wavelengths at

A

280 nm

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6
Q

what is the 3 and 1 letter code for selenocysteine

A

sec u

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7
Q

what is the 3 and 1 letter code for pyrrolysine

A

pyl o

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8
Q

how do biological systems ensure pH changes do not exceed the optimal range

A

buffer

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9
Q

what does the henderson equation describe

A

shape of the titration curve for all weak acids

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10
Q

what does the henderson equation relate

A

pH pka buffer concentration

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11
Q

what is the name for proteins with prosthetic groups

A

conjugated proteins

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12
Q

what information is there in a sequence

A

structural info (not 100%) but secondary, transmembrane helices, signal peptide sequences

cell localization

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13
Q

what do sequence alignments provide

A

function, structure and evolutionary info

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14
Q

what do gaps represent at the genetic level

A

insertions or deletions

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15
Q

what do gaps represent at the structural level

A

loops

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16
Q

degree of similarity in sequence alignments represents…..

A

length of time since divergence

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17
Q

orthologs arise out of ….

A

speciation events

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18
Q

paralogs arise out of…..

A

gene duplication events

19
Q

what are compounds separated by in differential centrifugation

A

sedimentation rate

20
Q

which complexes sediments first in differential centrifugation

A

large ones

21
Q

what kind of process is density centrifutation

A

equillibirum

22
Q

how is the eluent monitored in chromatography

A

light absortbance 280 nm

23
Q

what does the migration rate in electrophoresis depend on

A

charge/mass ratio

24
Q

which chemical breaks disulfide bonds

A

DTT

25
Q

where is the net dipole pointing in a peptide bond

A

towards the oxygen

26
Q

what is the shape of the peptide bond?

A

planar

27
Q

what is the bond angle in an extended chAIN

A

180

28
Q

describe the H-bonding patterns in stable forms of secondary structures?

A

repeating

29
Q

describe the difference in antiparallel vs parallel beta sheets

A

repeat period is shorter for paraellel
H-bonding pattern is different

30
Q

are beta sheets planar?

A

nah

31
Q

what are beta turns characterized by

A

backbone H-bonds

32
Q

what is a use for beta turns

A

connect antiparallel beta strands

33
Q

what ultimately determines tertiary structure

A

sequence & environment

34
Q

which forces are most critical in determining tertiary structure

A

non-covalent

35
Q

what does x-ray crystallography provide

A

info about electron density, used

36
Q

what does x-ray crystallography provide

A

info about electron density, used TO BUILD MODELS

37
Q

what is the crystal used to generate in x-ray crystallography?
what do these do

A

diffraction pattern

38
Q

what is the crystal used to generate in x-ray crystallography?
what do these do

A

diffraction pattern3
3d electron density map revealing location of atomic nuclei

39
Q

what are the pros of xray crystallography

A

detailed
rapid
large

40
Q

what are the cons of xray crystallography

A

crystal growth
diffraction
noH
static

41
Q

what does magnetic coupling provide information about

A

distance between atoms

42
Q

what are the pros of protein NMR

A

dynamic
in solution

43
Q

what are the cons of protein NMR

A

difficult for large
synthesis of peptides containing isotopes can be expensive