lecture 5 Flashcards

1
Q

valine has what side group as a side chain?

A

isopropyl

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2
Q

leucine has what as a side chain?

A

isobutyl

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3
Q

isoleucine has what as a side chain?

A

isobutyl

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4
Q

which amino acid has the largest side chain?

A

tryptophan

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5
Q

what is responsible for 280nm absorbance?

A

trytophan

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6
Q

which 2 amino acid has amphiphatic character?

A

tyrosine, threonine

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7
Q

what properties do trytophan have?

A

fluorescent

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8
Q

what measure absorbance? and which amino acid has highest?

A

beers law trytophan

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9
Q

which amino acids are sites of post translational activity?

A

threonine and serine

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10
Q

which amino acids so 0 glycosylation occur?

A

threonine and serine

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11
Q

what type of bond does cyteine form with cysteine?

A

covalent bond

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12
Q

what is most reactive group in proteins?

A

sulfhydryl

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13
Q

which amino acid has nucleophilic activity?

A

cysteine

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14
Q

cysteine must be what for effective anaylsis? it also reacts with what?

A

alkylated. metal ions

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15
Q

what is precursor to antioxidant glutathione?

A

cysteine

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16
Q

which aa can participate in acid/base reactions?

A

histidine

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17
Q

which amino acid has guanino group? and what does it do?

A

arginine, can interrupt protein structure

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18
Q

aa for deamidation reactions (protein ageing)

A

glutamine

19
Q

esterification reaction possible in which aa?

A

glutamate and aspartate

20
Q

which aa has cyclic imino acid?

A

proline

21
Q

amide bond resonance allows for what in the peptide bond?

A

stability and planar character

22
Q

which bonds in the peptide bond can rotate?

A

phi and psi

23
Q

phi is what?

A

in between N and alpha carbon

24
Q

psi is what

A

in between alpha carbon and carbon

25
Q

when it comes to forming peptide bond, equilibrium favors what? and kinetics are stable for how many years?

A

hydrolysis instead of synthesis. 1000

26
Q

what does phi bond prefer to be?

A

-120

27
Q

in alpha helices, how many residues separate h bonding atoms between N and C=O? residues rise at ____A and rotate ____. pitch is ____A

A

3.6, 1.5, 100 degrees, 5.4

28
Q

describe feeling of alpha and examples

A

stiff and rigid. fibrin (blood clots), keratin (hair), cytoskeleton, porcupine quills, tropomyosin (muscle)

29
Q

ferritin is what type of helice?

A

alpha

30
Q

which beta sheet is more stable and why?

A

antiparallel because of shorter hydrogen bonds between the nitrogen and C=O.

31
Q

when forming a loop what do you find?

A

glycine, proline and alanine.

32
Q

barrels are used usually for what?

A

nuclear pore complexes, allowing ions to pass through

33
Q

hairpin turn is what kind of sheer?

A

beta

34
Q

are omega loops common?

A

no

35
Q

which amino acids are no favored for alpha helices?

A

valine, isloleucine, threonine. serine, aspartic acid, asparagine

36
Q

explaine role proline plays in sheets?

A

disrupts alpha and beta sheets, so it is found in the turns usually in a cis formation

37
Q

urea does what to proteins?

A

denatures them by disrupting the water bonds.

38
Q

explain difference between simple dimer and hetero tetramer

A

dimer is quaternary structure with dimer of identical subunites. hetero tetramer is composed of different chains

39
Q

structural plasticity allows for what in hemoglobin?

A

cooperative oxygen binding

40
Q

what is a newtonian fluid?

A

viscosity is constant, even when flowing. when one pushes, viscosity does not change. examples are water, milk, vegetable oils, fruit juices, sugar, and salt solutions

41
Q

explain non newtonian fluid

A

viscosity changes when applied force changes. shear thinning- viscosity decreases when force is applied to the fluid. examples- latex paint, molasses, ketchup and saliva

42
Q

what is the Ph of saliva?

A

7.4

43
Q

what allows saliva to act as a lubricative film?

A

glycoproteins