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Biomol lecture > Amino Acids > Flashcards

Amino Acids Flashcards

Quiz. Exam. If it's in His Will, then may His will be done

1
Q

What are the essential amino acids?

A

Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine

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2
Q

What are the non-essential amino acids?

A

Alanine
Arginine
Asparagine
Aspartic Acid
Cysteine
Glutamic acid
Glutamine
Glycine
Proline
Selenocysteine
Serine
Tyrosine

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3
Q

only unique feature in each amino acid

A

R-group

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4
Q

two mirror image forms

A

L and D

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5
Q

With only very minor exceptions, every amino acid found in cells and proteins are in the ___________

A

L configuration

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6
Q

What are the classifications of R-groups?

A

Non-Polar
Carboxyl
Amine
Aromatic
hydroxyl
other

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7
Q

What are the amino acids that has Non-Polar R-groups?

A

Alanine
Glycine
Isoleucine
Leucine
Methionine
Proline
Valine

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8
Q

What are the amino acids that has carboxyl R-groups?

A

Aspartic Acid
Glutamic Acid

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9
Q

What are the amino acids that has Amine R-groups?

A

Arginine
Histidine
Lysine

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10
Q

What are the amino acids that has aromatic R-groups?

A

Phenylalanine
Tryptophan
Tyrosine

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11
Q

What are the amino acids that has hydroxyl R-groups?

A

Serine
Threonine
Tyrosine

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12
Q

What are the amino acids that has other R-groups?

A

Asparagine
Cysteine
Glutamine
Selenocysteine
Pyrrolysine

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13
Q

source of energy for cells

A

catabolism of amino acids

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14
Q

produce intermediates that can be turned into glucose

A

glucogenic

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15
Q

intermediates are made into acetyl-CoA

A

ketogenic

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16
Q

What are amino acids that are ketogenic

A

Lysine
Leucine

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17
Q

What are amino acids that are glucogenic

A

Arginine
Histidine
Proline
Glutamine

Glutamate

Methionine
Valine

Asparagine
Apartate

Alanine
Cysteine
Glycine
Serine

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18
Q

Amino acids that can be ketogenic and glucogenic

A

Tryptophan
Tyrosine
Phenylalanine
Threonine
Isoleucine

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19
Q

common alterations in post translational modifications

A

phosphorylation of hydroxyl groups
lysine, proline, and histidine can have hydroxyls added to amines in their R-groups
addition of fatty acids isoprenoid, acetyl, methyl, iodine, carboxyl, and sulfates

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20
Q

Tyrosine is precursor of

A

Epinephrine
thyroid hormones
L-dopa
Dopamine

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21
Q

Tryptophan is precursor of

A

serotonin

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22
Q

Histidine is precursor of

A

Histamine

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23
Q

polymers of amino acids

A

proteins

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24
Q

Amino acids are linked to each other by _______

A

peptide bonds

25
Q

carboxyl group of one amino acid is bind to another amino group with the ____________-

A

loss of water molecule

26
Q

chain made up of few amino acids linked together

A

oligopeptide

27
Q

oligo means

A

few

28
Q

atypical protein which is made up of many amino acids

A

polypeptide

29
Q

poly means

A

many

30
Q

end of peptide that has free amino group

A

N-terminus (for NH2)

31
Q

end of peptide with free carboxyl

A

C-terminus (for carboxyl)

32
Q

workhorses of the cell

A

proteins

33
Q

mediate signaling

A

proteins

34
Q

diversity of proteins

A

20n amino acids

35
Q

unique sequence or order of amino acids

A

primary structure

36
Q

dictates 3D conformation the folded protein will have

A

primary structure

37
Q

include a-helix and b-strands

A

secondary structure

38
Q

interactions between close amino acids gives rise to

A

secondary structure

39
Q

Secondary structures are predicted by

A

Linus Pauling
Robert Corey
Herman Branson

40
Q

how many amino acids per turn of a-helix

A

3.6 amino acids

41
Q

helices of amino acids are predominantly

A

right handed

42
Q

helices of glycines are

A

left handed

43
Q

form between C=O and N-H groups in polypeptide backbone

A

hydrogen bonds

44
Q

primary forces stabilizing a-helix

A

hydrogen bonds

45
Q

describe parameters of helix

A

rise
repeat
pitch

46
Q

no. of residues in a helix before it begins to repeat itself

A

repeat

47
Q

distance the helix elevates with addition of each residue

A

rise

48
Q

distance between complete turns

A

pitch

49
Q

stability of a-helix is enhanced by presence of amino acid

A

aspartate

49
Q

end amino acids are separated by one peptide bond

A

δ-turns

50
Q

separation by two peptide bonds

A

γ-turns

51
Q

separation by 3 peptide bonds

A

β-turns

52
Q

separation by 4 peptide bonds

A

α-turns

53
Q

separation by 5 peptide bonds

A

π-turns

54
Q

most common form

A

β-turns

55
Q

theoretical but unlikely due to steric limitations

A

δ-turns

56
Q

fourth most abundant secondary structure in proteins, constituting about 10-15% helices

A

310 helix (10 amino acids in 3 turns)

57
Q

special type of a-helix

A

π-turns

58
Q

a-helix with an extra amino acid stuck in the middle of it

A

π-turns

Biomol lecture (4 decks)

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