Topic 2 Flashcards

Amino Acids

1
Q

structure of amino acid

A
carboxyl group
amino group
alpha-carbon center
hydrogen
variable side chain
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2
Q

chirality

A

alpha-carbon bound to 4 different groups; all amino acids are chiral except glycine

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3
Q

amphoteric

A

ability to react as an acid or base due to carboxyl and amino groups

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4
Q

peptide bonding

A

when he carboxyl group of one molecule reacts with the amino group of another, releasing water

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5
Q

stereoisomerism

A

when two molecules have the same atoms, but arranged differently spatially.

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6
Q

human amino acid stereoisomerism

A

only the L-amino acids are used to make proteins

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7
Q

amino acid classification

A

polar/non-polar
aromatic
+/- charged
hydrophobic/philic

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8
Q

non-polar R-groups

A
glycine
alanine
proline
valine
leucine
isoleucine
methionine
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9
Q

aromatic R-groups

A

phenylalanine
tyrosine
tryptophan
histidine (?)

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10
Q

polar uncharged R-groups

A
serene
threonine
cysteine
asparagine
glutamine
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11
Q

polar (+) R-groups

A

lysine
argentine
histidine

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12
Q

polar (-) R-groups

A

aspartate

glutamate

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13
Q

branched chain R-groups

A

valine
leucine
isoleucine

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14
Q

acidic R-groups

A

aspartic acid/aspartate

glutamic acid/glutamate

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15
Q

alkaline R-groups

A

lysine
arginine
histidine

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16
Q

amide R-groups

A

asparagine

glutamine

17
Q

hydroxyl R-groups

A

serine
threonine
tyrosine

18
Q

achiral R-group

A

glycine

19
Q

hydrophilic R-groups

A

all of the polar groups

20
Q

sulfur R-groups

A

cysteine

methionine

21
Q

zwitterion

A

predominates at neutral pH

amphoteric

22
Q

isoelectric pH (pI)

A

pH at which net charge is 0

23
Q

titration of amino acids importance

A

net charge of the molecule at various ionic environments which has implication on

  1. biochemical reaction characteristics at various ionic conditions that may occur at different situations arising from normal reactions
  2. three dimensional spatial orientation of the molecule to interacted with another
  3. development of certain diseases
24
Q

amino acid polymerization

A

condensation reaction forming a peptide bond

25
Q

protein interactions

A

functional groups of molecules can interact with amino acid side chains and produce hydrogen bonds

26
Q

modification of amino acid R-group structure

A
  1. regulate biochemical functions
  2. form signaling molecules
  3. helps in targeting or anchoring to membrane
  4. enhance protein-protein interactions
27
Q

covalent modification of amino acid structures

A

hydroxylation: pro, lys
carboxylation: glu
methylation
acetylation: lys
phosphorylation: ser, thr, tyr
carb moieties
lipid moieties

28
Q

O-glycosylation

carb moieties

A

serine
threonine
tyrosine

29
Q

N-glycosylation

carb moieties

A

asparagine

30
Q

lipid moieties

A

cysteine

glycine

31
Q

uncommon amino acid modifications

A
4-hydroxyproline
5-hydroxylysine
6-N-methyllysine
γ-carboxyglutamate
selenocysteine