amino acid structure and function Flashcards

1
Q

what isomers are usually dealt with in biology

A

L isomers

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2
Q

hydrophobic amino acids

A
glycine
alanine
proline
valine
leucine
isoleucine
methionine
tryptophan
phenylalanine
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3
Q

polar amino acids

A
serine
threonine
tyrosine
asparagine
glutamine
cysteine
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4
Q

which amino acids can participate in redox rxns?

A

cysteine

disulfide linkages

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5
Q

charged (+) amino acids

basic

A

lysine
arginine
histidine

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6
Q

charged (-) amino acids

acidic

A

aspartate (aspartic acid)

glutamate (glutamic acid)

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7
Q

small amino acids

A

alanine
glycine
cysteine
serine

proline
threonine
aspartic acid
asparagine

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8
Q

medium amino acids

A

valine
histidine
glutamic acid
glutamine

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9
Q

large amino acids

A
isoleucine
leucine
methionine
lysine
arginine 

tyrosine
tryptophan
phenylalanine

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10
Q

essential amino acids

A

humans cannot synthesize; cannot make or cannot make enough

histidine
lysine
tryptophan
isoleucine
phenylalanine
valine
leucine
threonine

consumption > production:
arginine
methionine

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11
Q

nonessential amino acids

A

humans can synthesize dev novo

alanine
cysteine
glycine
asparagine
glutamine
proline
aspartic acid
glutamic acid 
serine

secondary synthesis:
tyrosine (can make it, but make it from a nonessential amino acid-phenylalanine

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12
Q

mnemonic for essential amino acids

A

Pvt Tim Hall (first letter of full name)

P henylalanine (Phe, F)
V aline (Val, V)
T ryptophan (Trp, W)
T hreonine (Thr, T)
I soleucine (Ile, I) 
M ethionine (Met, M)
H istidine (His, H)
A rginine (Arg, R)
L ysine (Lys, K)
L eucine (Leu, L)
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13
Q

proteinogenic amino acids

A

are used to make proteins from the genetic code

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14
Q

nonproteinogenic amino acids

A

are not decoded from the genome

e.x. post-translational modifications (phosphorylation for example)

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15
Q

21st amino acid

A

Selenocysteine (Sec, U)

pKa = 5.2
synthesized from serine

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16
Q

selenocysteine can be processed to:

A

selenomethionine in plants, algae, and yeast

and alanine in animals

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17
Q

stop codon for selenocysteine

A

UGA (opal)

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18
Q

selenocysteine is found in

A

all 3 domains of life (bacteria, archea, and eukaryea)

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19
Q

selenocysteine uses its own

A

tRNA and SECIS (selenocysteine insertion sequence)

20
Q

proteins that incorporate Sec are called

A

selenoproteins

21
Q

selenoproteins are important for good health:

A

reduce oxidative stresses in conjunction with vitamin E

required in cerebellum neurons (growth and coordination)

moderate inflammatory responses (may reduce IBD)

22
Q

what happens to a selenoprotein when Sec is not available

A

usually a stop codon –> proteins ends up truncated

23
Q

selenium deficiency results in

2.

A
  1. myopathies

keshan disease (cardiomyopathy

  • caused by not enough selenium in the diet
  • oxidative stress is disinhibited
  • treated with Se supplements

statin intolerance (rhabdomyolysis-muscle death)

  • statins inhibit Sec-tRNA
  • treated by discontinuing statin
  1. Immune-incompetence
24
Q

statins are drugs that

A

block the formation of cholesterol in the liver

25
Q

too much selenocysteine results in

A

hair and nail brittleness, “garlic breath”

gastrointestinal/neurological leions

myopathies, renal failure, and death

26
Q

22nd amino acid

A

pyrrolysine (Pyl, O)

made by combining 2 lysines

27
Q

stop codon for pyrrolysine

A

UAG (amber)

28
Q

pyrrolysine is found

A

in some prokaryotes, all are methanogens

29
Q

pyrrolysine uses its own

A

tRNA

30
Q

several members of the human intestinal microbiome make/use Pyl) including

A

methanomassiliicoccus luminyensis (arahaea)

bilophila wadsorthia (eubacteria)

31
Q

nonproteinogenic amino acids include

A

post-translation additions to proteinogenic amino acids

D-enantiomers

metabolism intermediates

pre-biotic or extraterrestrial origin

proteins made by non-riboosomal protein synthesis

32
Q

A/Adenylation

A

activation carboxyl

33
Q

PCP/Peptidyl carrier

A

elongation intermediate

34
Q

C/Condensation

A

peptide bond formation

35
Q

TE/Thioesterase

A

release of cyclization

36
Q

most antibiotics are made by

A

non-ribosomal protein synthesis

37
Q

newest class of antibiotics

A

odilorhabdins

38
Q

statins are made by

A

polyketide synthesis (PKS)

39
Q

primary structure

A

chain of amino acids

40
Q

secondary structure

A

local folding of the polypeptide chain, connected by hydrogen bonds

alpha helices and beta sheet

41
Q

tertiary structure

A

folding of the secondary structure, connected by disulfide linkages

42
Q

quaternary structure

A

interaction of multiple peptides

43
Q

polypeptide chains start from _____ and go towards _____

A

amino side

carboxyl side

44
Q

peptide bond

A

bond between carbon and nitrogen

45
Q

because amino acids are joined by a single bond,

A

rotation is possible