Amino Acids Flashcards

(56 cards)

1
Q

Polar (neutral) amino acids

A
Serine             (Ser, S)
Threonine      (Thr, T)
Asparagine    (Asn, N)
Glutamine      (Glen, Q)
Glycine           (Gly, G)

Cysteine (Cys, C)
Tyrosine (Tyr, Y)

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2
Q

Polar (acidic) amino acids

A
Glutamic Acid    (Glu, E)
Aspartic Acid     (Asp, D)
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3
Q

Acronym for polar (neutral) amino acids

A

STAGG CT

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4
Q

Acronym for polar (acid) amino acids

A

GA

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5
Q

Acronym for polar (base) amino acids

A

HAL

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6
Q

Polar (basic) amino acids

A

Histidine (His, H)
Arginine (Arg, R)
Lysine (Lys, K)

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7
Q

Non-polar (hydrophobic) amino acids

A
Valine               (Val, V)
Alanine            (Ala, A)
Methionine    (Met, M)
Leucine           (Leu, L)
Isoleucine       (Ile, I)
Proline             (Pro, P)
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8
Q

Valine abbreviation

A

Val (V)

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9
Q

Alanine abbreviation

A

Ala (A)

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10
Q

Leucine abbreviation

A

Leu (L)

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11
Q

Proline abbreviation

A

Pro (P)

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12
Q

Methionine abbreviation

A

Met (M)

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13
Q

Tryptophan abbreviation

A

Try (W)

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14
Q

Phenylalanine abbreviation

A

Phe (F)

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15
Q

Isoleucine abbreviation

A

Ile (I)

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16
Q

Glycine abbreviation

A

Gly (G)

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17
Q

Serine abbreviation

A

Ser (S)

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18
Q

Asparagine abbreviation

A

Asn (N)

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19
Q

Glutamine abbreviation

A

Gln (Q)

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20
Q

Threonine abbreviation

A

Thr (T)

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21
Q

Cysteine abbreviation

A

Cys (C)

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22
Q

Tyrosine abbreviation

A

Tyr (Y)

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23
Q

Aspartic acid abbreviation

24
Q

Glutamic acid abbreviation

25
Lysine abbreviation
Lys (K)
26
Arginine abbreviation
Arg (R)
27
Histidine abbreviation
His (H)
28
Amino acid with a pKa value close to neutral
His (H): pKa (imidazole) = 6.0 Cys (C): pKa (sulfahydryl) = 8.3
29
pKa value close to pH value serves as
Buffer
30
Peptidyl bond tasks place on
Ribosome
31
Non-covalent interactions that stabilize a protein structure
Hydrogen Ionic Hydrophobic Van der Waals
32
One polypeptide chain
Monomeric protein
33
More than one polypeptide chain
Multimeric protein
34
One kind polypeptide chain
Homomultimer
35
Two or more different polypeptide chains
Heteromultimer
36
Hemoglobulin structure
Heterotetramer (2 alpha and 2 beta)
37
Amino acids linked together by peptide bonds (structure)
Primary
38
Regions of polypeptide chain coiled into a-helix (structure)
Secondary
39
Final folding of polypeptide chain - region associate with each other (structure)
Tertiary
40
Two or more peptide chains that form functional protein (structure)
Quaternary
41
Secondary structure (consists of)
Alpha helix | Beta sheets
42
Bonds of secondary protein structure
Hydrogen
43
Bonds of primary protein structure
Peptidyl bond (covalent)
44
Bonds of quaternary proteins
Hydrogen Ionic van der Waals
45
Bonds of tertiary protein structures
``` Salt bridges (disulfide) Ionic interactions ```
46
Ionic interactions occur
On protein structure
47
Stabilizes folding
Disulfide bonds (covalent)
48
Bonds that drive protein folding
Hydrophobic interactions
49
Functional diversity of protein structures derives from
1) Number of folded structures | 2) Chemistry of side chains
50
Globular proteins consist most of
Helixes and sheets
51
Carbon atom of amino acid (structure)
Central tetrahedral
52
Sequence of amino acids if encoded by
Nucleotide sequence of DNA
53
Protein structure is read from
Amine group to carboxyl group
54
Bonds that will stabilize folding
Covalent disulfide
55
Reason for protein folding into 3D structures
Hydrophilic and hydrophobic
56
Surface elements of globular protein structure responsible for
Enzyme-substrate interactions Cell signaling Immune responses