Amino Acids Flashcards

1
Q

how many amino acids incorporated into proteins

A

20

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2
Q

all but one amino acid exist in this type of form

A

L-form

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3
Q

which amino acid does not exist in the L-form

A

glycine

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4
Q

all AA can act as an Acid or base

we call this:

A

amphoteric

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5
Q

what is the pneumonic for the essential amino acids

A

PVT TIM HALL

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6
Q

list the essential amino acids

A
phenylalanine
valine
tryptophan
threonine
isoleucine
methionine
histidine
arginine
leucine
lysine
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7
Q

when is histidine essential

A

in a child but not an adult

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8
Q

what are the purely ketogenic amino acids

A

leucine and lysine

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9
Q

lysine is a precursor to

A

carnitine

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10
Q

what does carnitine do

A

takes FA into mitochondria for B-oxidation

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11
Q

the aromatic amino acids are

A

phenylalanine
tyrosine
tryptophan

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12
Q

the sulfur-containing amino acids are

A

cysteine
methionine
cystine

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13
Q

what is cystine

A

2 cysteines linked together

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14
Q

what doesn’t Glycine contain in order to exist in the “L-form”

A

a chiral carbon

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15
Q

what is a chiral carbon

A

different compounds at each binding site

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16
Q

what are the branched chain amino acids

A

valine
isoleucine
leucine

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17
Q

in which disease can they not break down branched chain AA

A

maple syrup urine disease

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18
Q

the acidic amino acids are

A
aspartic acid (aspartate)
glutamic acid (glutamate)
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19
Q

FYI: aspartame contains aspartic acid= XS

A

neurotoxic

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20
Q

the basic amino acids are

A

histidine
lysine
arginine

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21
Q

when do basic amino acids have the greatest positive net charge

A

at NORMAL pH of blood

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22
Q

what is the limiting AA for wheat

A

lysine

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23
Q

what is the limiting AA for rice

A

lysine

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24
Q

what is the limiting AA for legumes

A

tryptophan

25
what is the limiting AA for maize
lysine and tryptophan
26
what is the limiting AA for pulses
methionine (or cysteine)
27
what is the limiting AA for egg, chicken
none | the reference for absorbable protein
28
explain the amino acid derivative for phenylalanine
Phenylalanine -> Tyrosine->L-dopa or T3, T4 L-Dopa->dopamine->norepinephrine->epinephrine L-Dopa-> melanin
29
deficiency in phenylalanine hydroxyls leads to
phenylketonuria (PKU)
30
dopamine, norepinehprine, epinephrine are all
catecholamines
31
what happens if body cannot convert L-Dopa into melanin
albinism
32
what is the amino acid derivative for histidine
histidine->histamine
33
what is the amino acid derivative for tryptophan
Tryptophan->Serotonin->Melatonin | Tryptophan->Niacin->Nicotinamide
34
how man grams of protein does the body need for every 10 kilograms
8
35
pH when an amino acid has no net electrical charge (neutral)
isoelectric point
36
an amino acid at its isoelectric point
zwitter ion
37
tripeptide of Glycine + Glutamate + Cysteine
glutathione
38
this is a mineral for enzyme Glutathione Peroxidase
selenium
39
2 polypeptide chains linked by disulfide bonds
insulin
40
insulin is not part of what?
animal cell membrane | but it helps glucose enter the cell
41
give an example of a polypeptide hormone
insulin | glucagon
42
give an example of a catecholamine
epinephrine | norepinephrine
43
give an example of a steroid
testosterone cortisol estrogen progesterone
44
the characteristic bond of all proteins is the
peptide bond
45
what kind of bond is the peptide bond
amide bond
46
what are aka's for the peptide bond
C-N bond | Carboxyl-Amino bond
47
how many protein structures are there
4
48
what is a primary structure
linear sequence fo amino acids
49
what is a secondary structure
alpha helices and beta pleated sheets
50
in a secondary structure, what holds the structures together
hydrogen bonds between atoms of the polypeptide backbone
51
give an example of secondary structures
fibrous protein's collagen and silk | 2 DNA strands together
52
what is the tertiary structure
folding of a single polypeptide chain in solution
53
what is the classic example of a globular protein with tertiary structure
myoglobin
54
what kind of bonds exist in the tertiary structure
disulfide bonds
55
what is the quaternary structure
association of two or more polypeptide chains to make a functional protein
56
what is the classic example of a quaternary structure
hemoglobin(alpha2beta2)
57
what bonds exist int eh quarternary structure
hydrogen and disulfide
58
hemoglobin is also what type of compound
Allosteric compound | oxygen will change conformational shape
59
what do disulfide bonds do
they connect the light and heavy chains of an antibody