amino acid structure and function Flashcards

(45 cards)

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
too much selenocysteine results in
hair and nail brittleness, "garlic breath" gastrointestinal/neurological leions myopathies, renal failure, and death
26
22nd amino acid
pyrrolysine (Pyl, O) made by combining 2 lysines
27
stop codon for pyrrolysine
UAG (amber)
28
pyrrolysine is found
in some prokaryotes, all are methanogens
29
pyrrolysine uses its own
tRNA
30
several members of the human intestinal microbiome make/use Pyl) including
methanomassiliicoccus luminyensis (arahaea) bilophila wadsorthia (eubacteria)
31
nonproteinogenic amino acids include
post-translation additions to proteinogenic amino acids D-enantiomers metabolism intermediates pre-biotic or extraterrestrial origin proteins made by non-riboosomal protein synthesis
32
A/Adenylation
activation carboxyl
33
PCP/Peptidyl carrier
elongation intermediate
34
C/Condensation
peptide bond formation
35
TE/Thioesterase
release of cyclization
36
most antibiotics are made by
non-ribosomal protein synthesis
37
newest class of antibiotics
odilorhabdins
38
statins are made by
polyketide synthesis (PKS)
39
primary structure
chain of amino acids
40
secondary structure
local folding of the polypeptide chain, connected by hydrogen bonds alpha helices and beta sheet
41
tertiary structure
folding of the secondary structure, connected by disulfide linkages
42
quaternary structure
interaction of multiple peptides
43
polypeptide chains start from _____ and go towards _____
amino side carboxyl side
44
peptide bond
bond between carbon and nitrogen
45
because amino acids are joined by a single bond,
rotation is possible