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Biochemistry, genetics, and metabolism > aimno acids > Flashcards

aimno acids Flashcards

1
Q

Asp

A

aspartate, polar (aspartic acid-acid polar)

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2
Q

Glu

A

Glutamate, polar (glutamic acid-acid polar)

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3
Q

Tyr

A

Tyrosine, uncharged polar

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4
Q

Asn

A

Asparagine, uncharged polar

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5
Q

Gln

A

Glutamine, uncharge polar

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6
Q

Trp

A

Tryptophan, nonpolar

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7
Q

Cys

A

Cystein, uncharged polar

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8
Q

His

A

Histidine, basic polar

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9
Q

Ile

A

Isoleucine, nonpolar

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10
Q

Met

A

Methionine, nonpolar

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11
Q

Ser

A

Serine, uncharged polar

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12
Q

Val

A

Valine, nonpolar

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13
Q

Ala

A

Alanine, nonpolar

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14
Q

Gly

A

Glycine, nonpolar

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15
Q

Leu

A

Leucine, nonpolar

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16
Q

Pro

A

Proline, nonpolar

17
Q

Thr

A

Threonine, uncharged polar

18
Q

Arg

A

Arginine, Basic Polar

19
Q

Phe

A

Phenylalanine, nonpolar

20
Q

Lys

A

Lysine, basic polar

21
Q

Nonpolar Amino Acids

A 
alanine
Glycine
Isoleucine
Leucine
Methionine
Phenylalanine
Proline
Tryptophan
Valine

9

22
Q

uncharged Polar amino acids

A 
asparagine
cysteine
glutamine
serine
threonine
tyrosine

6

23
Q

Acidic polar amino acids

A

Aspartic acid

glutamic acid

24
Q

Basic polar amino acids

A

arginine
histidine
lysine

25
Q

What is special about methionin and tryptophan?

A

nonpolar amino acids who have something other than just carbon and hydrogen in the R group. Tryptophan has nitrogen, methionin has 1 sulfur group

26
Q

Maple Syrup Urine Disease

A

when the breakdown of Isoleucine, leucine, and valdine is disrupted. They are branched chain amino acids.

27
Q

What is special about phenylalanine

A

During normal catabolism, it is broken down into tyrosine. Patients with a defective step in this pricess suffer from PKU, can cause retardation

28
Q

What is special about tryptophan?

A

it is the precursor for serotonin, which serves as an important neurotransmitter with roles in pain perception, regulation of sleep, appetite, temperature, blood pressure, cognitive functions, and mood.

29
Q

What is important about glycine

A

Found in collagen, 1st in sequence of 3. has the smallest R group. If it gets substituted by another amino acid, the resulting bulkier R group disrupts the normal collagen structure, this is called osteogenesis imperfecta. can cause brittle bones

30
Q

What is special about proline?

A

cyclic, rigid

31
Q

What is special about methionine?

A

serves as a methyl group donor in many methylation reactions in biochemistry

32
Q

What contributes to the overall charge on a polypeptide?

A

Charged amino acids

33
Q

What amino acids MAY be phisphorylated?

A

Serine, Threonine, and Tyrosine

34
Q

What is tyrosine a precurosor for?

A

catecholamines

Biochemistry, genetics, and metabolism (11 decks)

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