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M2M section 1 > amino acids and proteins > Flashcards

amino acids and proteins Flashcards

1
Q

nonpolar aliphatic AA

A

glycine alanine valine leucine isoleucine methionine

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2
Q

aromatic

A

phenylalanine tyrosine tryptophan

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3
Q

polar and uncharged

A

serine proline threonine cytosine asparagine glutamine

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4
Q

polar and positive

A

histidine arginine lysine

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5
Q

polar and negative

A

aspartate and glutamate

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6
Q

example of a molecule that uses disulfide bridges

A

insulin

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7
Q

scurvy is when you screw up what modification of what amino acid

A

vitamin c needed to turn proline into hydroxyproline

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8
Q

who cares about carboxylated glutamine and what does it need and what drug helps when this is fucked up

A

vitamin k- important for clotting- warfarin (aka coumadin)

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9
Q

force of H bonds

A

1-7 kj/mol

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10
Q

alpha helix is how many residues per turn and how many angstroms

A

3.6 r/t and 5.4 angstroms

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11
Q

what do you get when your glycosylation pathways are genetically fucked up

A

congenital disorder of glycosylation

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12
Q

what is gleevec and who uses it

A

tyrosine kinase inhibitor used to treat CML

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13
Q

what is bortezomib and why do we use it

A

protease inhibitor to treat multiple myeloma

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14
Q

3 covalent bonds in peptide backround- which is phi, which is psi, and which has double bond character

A
  1. Ca- carbonyl of AA1 (psi), 2. Carbonyl C of AA1- amide N of AA2 (double bond character, phi), 3. aminde N and Ca of AA2
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15
Q

what determines secondary structure

A

H bonding between amide N and carbonyl oxygen

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16
Q

what is the 2ndary structure of collagen

A

triple L handed helix

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17
Q

in the alpha helix, which AAs H bond to each other and which are on top of each other

A

N bonds to N+4, 1st and 8th are stacked

18
Q

what 2 AAs can’t form alpha helices

A

glycine and proline

19
Q

hemoglobin is mostly what 2ndary structure

A

alpha helix

20
Q

thalassemia is caused by what defect in secondary structure

A

unstable alpha helices in hemoglobin

21
Q

give an example of a protein thats mostly beta sheets

A

immunoglobulin

22
Q

how do you monitor a proteins secondary structure

A

circular dichroism

23
Q

2 major types of tertiary structures

A

fibrous and globular

24
Q

fibrous proteins tend to have what unique characteristic regarding their 2ndary strucure

A

EITHER alpha or beta- not mixed

25
Q

what is the role and solubility of fibrous proteins

A

insoluble, strucural/protetive

26
Q

most proteins in the body have what tertiary structure

A

globular

27
Q

globular proteins solubility?

A

water or lipid soluble

28
Q

what are the most frequently found AAs in turns and loops

A

glycine and proline

29
Q

how many polypeptides are in hemoglobin

A

4

30
Q

what does Kd represent

A

disassociation constant aka binding strength of a protein and ligand

31
Q

what are the 2 states of hemoglobin

A

tense and relaxed

32
Q

2 major ways to determine protein structure

A

crystallography–> Xray diffraction and NMR usig magnetic resonance

33
Q

what protein can totally refold on its own specifically

A

ribonuclease A

34
Q

two major classes of chaperones

A

Hsp70 and GroEL

35
Q

what does protein disulfide isomerase do

A

catalyzes the exchange between free cysteines and disulfide bonds to make the right disulfide bonds

36
Q

prolyl isomerase does what

A

catalyzes the conversation between trans and cis proline

37
Q

prion disease means changing from ___ secondary structure to ___

A

alpha helix– beta sheet

38
Q

3 major protein purification approaches

A

gel filtration chromatography (sep based on size), ion exchange chromatography( separates based on charge differences) affinity chromatography (utilizes proteins affinity to bind certain ligands)

39
Q

how do you determine the mass of a protein

A

mass spectrometry

40
Q

what does Edman degradation do

A

determines the N terminal sequence of a protein

M2M section 1 (14 decks)

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