Amino acids + proteins Flashcards

1
Q

amino acids are all in L-form except

A

glycine

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2
Q

amphoteric

A

acid or basic

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3
Q

essential amino acids

A
phenylalanine
valine
tryptophan
threonine
isoleucine
methionine
histidine (arginine)
leucine (maple syrup disease)
lysine
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4
Q

semi-essential

A

histadine

arginine

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5
Q

aromatic ring

A

aka benzine ring
phenylalanine
tryptophan
TYROSINE

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6
Q

basic (positive charge at nuetral ph)

A

histidine
arginine
lysine

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7
Q

neutral

A

serine
threonine
asparagine
glutamine

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8
Q

sulfur containing

A

methionine

cysteine

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9
Q

not glucogenic

A

leucerine

lysine

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10
Q

branch chain

A

leucine
isoleucine
valine

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11
Q

acidic

A

glutamate

aspartate

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12
Q

aliphatic chain

from less hydrophilic to more hydrophilic

A
glycine
alanine
valine
leucine
isoleucine
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13
Q

serotonin is precursor to

A

tryptophan

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14
Q

GABA is precursor to

A

glutamate

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15
Q

histamine is precursor to

A

histidine

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16
Q

creatine is precursor to

A

glycine and arginine

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17
Q

NAD is precursor to

A

tryptophan

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18
Q

what are amino acid food sources

A

meats, fish, eggs, dairy, peanut butter, grains

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19
Q

digestion of amino acids

  1. mouth
  2. stomach
  3. small intestine
A
  1. none, ptyalin
  2. pepsin, HCLM renin(infcancy and childhood only)
  3. trypsin, chymotrypsin, carboxypeptidase, amino peptidase, dipeptidase
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20
Q

what are the isoflavones in soy

A

genistein, daidzein, glycitein

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21
Q

what do legumes lack

A

methionine

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22
Q

which amino acids lack in grains

A

lysine, threonine and tryptophan

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23
Q

pathway of phenylalanine to epi

A

phenylalanine –> tyrosine –> l-dopa (also turns into melanin) –> dopamine –> nor epi –> epi

24
Q

aa metabolims route

A

trasamination then oxidative deamination

25
Q

where does removed ammonia go

A

carried to urea cycle by glutamate

26
Q

what are the left over carbon skeletons of aa

A
  1. glucogenic (form pyruvate or oxaloacetate to make glucose)
  2. ketogenic (form acetyl coa or acetoacetyl coa to make ketones)
27
Q

what makes glucose

A

pyruvate or oxoloacetate

28
Q

what makes ketones

A

acetyl coa or acetoacetyl coa

29
Q

what is the conversion of alanine

A

pyruvate (vice versa)

30
Q

what is the conversion of glutamine

A

glutamate (vice versa) a ketoglutarate

31
Q

what is the conversion of aspargine

A

aspartate

32
Q

what is the conversion of serine

A

pyruvate(vice versa)

33
Q

what are oxidized to make uric acid

A

purines

34
Q

what are the 3 aa that donate nitrogen for purines and pyrimidines

A

glutamate, aspartate, asparagine

35
Q

what are the 6 aa that muscle is able to oxidize

A

glutamate, aspartate, leucine, valine, isoleucine, asparagine

36
Q

aka for glucose alanine cycle

A

lactic acid cycle

cori cycle

37
Q

what does the muscle make during exercise

A

ammonia from amino acids

lactate from glucose

38
Q

what makes alanine

A

ammonia and lactte

39
Q

what does the liver do in the glucose alanine cycle

A

converts alanine back into lactate and ammonia

40
Q

what happens to ammonia and lactate in the glucose alanine cycle

A

ammonia –> urea

lactate –> glucose

41
Q

what process is it called when lactate becomes glucose

A

gluconeogenisis

42
Q

what is the last process of the glucose alanine cycle

A

glucose returns to the muscle via blood

43
Q

what is the function of the urea cycle

A

rids body of toxic ammonia

44
Q

what is the enzyme in the urea cycle

A

carbamoyl phosphate synthetase

45
Q

what does carbamoyl phosphate synthetase produce

A

carbamoyl phosphate

46
Q

what is the rate limiting enzyme in the urea cycle

A

carbamoyl phosphate synthase

47
Q

what does carbamoyl phosphate synthetase require

A

ATP and Mg

48
Q

what are the important intermediates in the urea cycle

A

fumarate, arginine, citrulline, ornithine, glutamate, aspartate

49
Q

what are the bonds between aa

A

peptide bond

50
Q

what does glucagon turn into

A

peptide hormone

51
Q

primary structure of proteins

A

number and sequence of amino acids; determines proteins structure

52
Q

secondary structure of proteins

A

alpha helix and beta pleated sheet

53
Q

aka for beta pleated sheet

A

beta bend

54
Q

tertiary structure of proteins

A

max fold for function

55
Q

quaternary structure of proteins

A

more than one chain

best ex. hemoglobin which has four chains