Amino Acids, Peptides, and Protein I Flashcards

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1
Q

Hydrophobic and non-polar amino acids

A
Valine
Isoleucine
Leucine
Methionine
Phenylalanine
Tryptophan
Cystine
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2
Q

hydrophilic and polar amino acids

A
argenine
lysine
aspartate
glutamate
asparagine
glutamine
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3
Q

acidic amino acids

A

aspartate

glutamate

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4
Q

basic amino acids

A

lysine
arginine
histidine

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5
Q

what may interactions between positive and negative R groups form?

A

salt bridge important for stabilization in proteins

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6
Q

what is a disulfide bond?

A

covalent linkage between two sulfer atoms specifically between cystine residues (thiol groups)

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7
Q

which amino acid has a sulfur bond but cannot participate in a disulfide bond?

A

methionine

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8
Q

where are disulfide bonds usually found within a folded protein?

A

on the inside because they are hydrophobic

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9
Q

what are the 6 major post-translational modifications that we need to know?

A
  1. hydroxylation of proline
  2. carboxylation of glutamate
  3. modification by acetylation or methylation
  4. glycosylation
  5. reversible phosphorylation/dephosphorylation
  6. ubiquination
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10
Q

what adds a hydroxyl group to proline residue?

A

prolyl hydroxylase

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11
Q

what is the predominate secondary structure in collagen and how is it formed?

A

proline helix

formed by multiple prolines and hydroxyprolines in a row

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12
Q

what is the cofactor of prolyl hydroxylase?

A

vitamin C

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13
Q

what disease results as a lack of vitamin C and which structure is affected?

A

scurvy, loss of integrity in connective tissues becase lack of proline hydroxylation

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14
Q

which enzyme adds a carboxyl group to the side chain of glutamate?

A

Gamma-glutamyl carboxylase

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15
Q

what is the co-factor of carboxylation of glutamate?

A

vitamin K

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16
Q

where is carboxylation of glutamate mostly found?

A

within clotting factors

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17
Q

what will a lack of vitamin K cause in regards to carboxylation of glutamate?

A

hemorrhage

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18
Q

how does waafarin work?

A

blood thinner that prevents clotting by inhibiting activity of gamma-glutamyl carboxylase

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19
Q

where does acetylation by HATs usually occur?

A

lysine residues of free tails of histones

20
Q

where does methylation usually occur and by which enzyme?

A

lysine and arginine residues on histones by methyltransferases

21
Q

what type of inhibitor is Vorinostat?

A

HDAC inhibitor

22
Q

what is the mechanism of Vorinostat?

A

prevents removal of acetyl groups from histones. Tumors usually use deacetylation to repress tumor suppresor genes.

23
Q

what is glycosylation?

A

attaching glycans (sugars) to proteins

24
Q

what are the 4 types of glycans?

A
  1. N-linked glycans
  2. O-linked glycans
  3. phospho-glycans
  4. C-linked glycans
25
Q

what amino acids to N-linked glycans attach to?

A

asparagine and arginine side chains

26
Q

what amino acids to O-linked glycans attach to?

A

serine, threonine, tyrosine, hydroxylysine, hydroxyproline side chains

27
Q

where do phospho-glycans attach?

A

phosphate of phospho-serine

28
Q

where do C linked glycans attach?

A

carbon on tryptophan side chain

29
Q

True of False

Glycosylation makes protein more polar

A

true

30
Q

what is the purpose of glycosylation?

A
  • proper protein folding
  • increased stability of secreted glycoproteins
  • cell to cell adhesion
  • role in recognition
31
Q

what genetic disease does disruption in N-glycosylation lead to?

A

Congenital disorder of glycosylation (CDG)

32
Q

what is the presentation of congenital disorder of glycosylation (CDG)?

A

developmental delay and hypertonia

33
Q

what mutation causes congenital disorder of glycosylation (CDG)?

A

PMM2 gene, autosomal recessive

34
Q

which amino acids does phosphorylation usually occur?

A

serine, threonine, tyrosine

phosphate group added to OH

35
Q

what does phosphorylation do?

A

activates or deactivates proteins and does reverse with dephosphorylation

36
Q

what is the target of Gleevac?

A

bcr-abl tyrosine kinase

37
Q

what disease is Gleevac used to treat?

A

Chronic myelogenous leukemia (CML)

38
Q

what is the mechanism of action of Gleevac?

A

kinase inhibitor: prevents bcr-abl tyrosine kinase from phosphoyrlating tyrosine by competitively binding to active site

39
Q

what is the most common type of modification of amino acids in cells?

A

ubiquination

40
Q

what is the function of ubiquination?

A

targets protein for destruction from the proteosome

41
Q

what is the process of ubiquination?

A

adds ubiquitin to lysine residues, addition of one recruits several more

42
Q

what disease does bortezomib treat?

A

multiple myeloma

43
Q

what kind of drug is bortezomib classified as?

A

proteasome inhibitor

44
Q

what is the mechanism of bortezomib?

A

boron atom in bortezomib binds to catalytic site of 26S proteasome with high affinity and specificity

45
Q

what is the theory of proteasome inhibition?

A

prevents degredation of pro-apoptotic factors permitting programmed cell death in cells dependent on suppression of pro-apoptotic pathways