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BIOCHEMISTRY Q1 > Amino Acids > Flashcards

Amino Acids Flashcards

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

A

Asp (D)

24
Q

Glutamic acid abbreviation

A

Glu (E)

25
Q

Lysine abbreviation

A

Lys (K)

26
Q

Arginine abbreviation

A

Arg (R)

27
Q

Histidine abbreviation

A

His (H)

28
Q

Amino acid with a pKa value close to neutral

A

His (H): pKa (imidazole) = 6.0

Cys (C): pKa (sulfahydryl) = 8.3

29
Q

pKa value close to pH value serves as

A

Buffer

30
Q

Peptidyl bond tasks place on

A

Ribosome

31
Q

Non-covalent interactions that stabilize a protein structure

A

Hydrogen
Ionic
Hydrophobic
Van der Waals

32
Q

One polypeptide chain

A

Monomeric protein

33
Q

More than one polypeptide chain

A

Multimeric protein

34
Q

One kind polypeptide chain

A

Homomultimer

35
Q

Two or more different polypeptide chains

A

Heteromultimer

36
Q

Hemoglobulin structure

A

Heterotetramer (2 alpha and 2 beta)

37
Q

Amino acids linked together by peptide bonds (structure)

A

Primary

38
Q

Regions of polypeptide chain coiled into a-helix (structure)

A

Secondary

39
Q

Final folding of polypeptide chain - region associate with each other (structure)

A

Tertiary

40
Q

Two or more peptide chains that form functional protein (structure)

A

Quaternary

41
Q

Secondary structure (consists of)

A

Alpha helix

Beta sheets

42
Q

Bonds of secondary protein structure

A

Hydrogen

43
Q

Bonds of primary protein structure

A

Peptidyl bond (covalent)

44
Q

Bonds of quaternary proteins

A

Hydrogen
Ionic
van der Waals

45
Q

Bonds of tertiary protein structures

A 
Salt bridges (disulfide) 
Ionic interactions
46
Q

Ionic interactions occur

A

On protein structure

47
Q

Stabilizes folding

A

Disulfide bonds (covalent)

48
Q

Bonds that drive protein folding

A

Hydrophobic interactions

49
Q

Functional diversity of protein structures derives from

A

1) Number of folded structures

2) Chemistry of side chains

50
Q

Globular proteins consist most of

A

Helixes and sheets

51
Q

Carbon atom of amino acid (structure)

A

Central tetrahedral

52
Q

Sequence of amino acids if encoded by

A

Nucleotide sequence of DNA

53
Q

Protein structure is read from

A

Amine group to carboxyl group

54
Q

Bonds that will stabilize folding

A

Covalent disulfide

55
Q

Reason for protein folding into 3D structures

A

Hydrophilic and hydrophobic

56
Q

Surface elements of globular protein structure responsible for

A

Enzyme-substrate interactions
Cell signaling
Immune responses

BIOCHEMISTRY Q1 (11 decks)

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