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
carboxyl group of one amino acid is bind to another amino group with the ____________-
loss of water molecule
26
chain made up of few amino acids linked together
oligopeptide
27
oligo means
few
28
atypical protein which is made up of many amino acids
polypeptide
29
poly means
many
30
end of peptide that has free amino group
N-terminus (for NH2)
31
end of peptide with free carboxyl
C-terminus (for carboxyl)
32
workhorses of the cell
proteins
33
mediate signaling
proteins
34
diversity of proteins
20n amino acids
35
unique sequence or order of amino acids
primary structure
36
dictates 3D conformation the folded protein will have
primary structure
37
include a-helix and b-strands
secondary structure
38
interactions between close amino acids gives rise to
secondary structure
39
Secondary structures are predicted by
Linus Pauling Robert Corey Herman Branson
40
how many amino acids per turn of a-helix
3.6 amino acids
41
helices of amino acids are predominantly
right handed
42
helices of glycines are
left handed
43
form between C=O and N-H groups in polypeptide backbone
hydrogen bonds
44
primary forces stabilizing a-helix
hydrogen bonds
45
describe parameters of helix
rise repeat pitch
46
no. of residues in a helix before it begins to repeat itself
repeat
47
distance the helix elevates with addition of each residue
rise
48
distance between complete turns
pitch
49
stability of a-helix is enhanced by presence of amino acid
aspartate
49
end amino acids are separated by one peptide bond
δ-turns
50
separation by two peptide bonds
γ-turns
51
separation by 3 peptide bonds
β-turns
52
separation by 4 peptide bonds
α-turns
53
separation by 5 peptide bonds
π-turns
54
most common form
β-turns
55
theoretical but unlikely due to steric limitations
δ-turns
56
fourth most abundant secondary structure in proteins, constituting about 10-15% helices
310 helix (10 amino acids in 3 turns)
57
special type of a-helix
π-turns
58
a-helix with an extra amino acid stuck in the middle of it
π-turns