Amino Acids,Peptides, & Proteins Flashcards

1
Q

molecules that contain two functional groups: an amino group and a carboxyl group

A

Amino Acids

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2
Q

20 alpha-amino acids

A

proteinogenic amino acids

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3
Q

has hydrogen atom as its R group, making it achiral

A

Glycine

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4
Q

only amino acid that has a R configuration

A

Cysteine

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5
Q

glycine, alanine, valine, leucine, isoleucine, methionine, and proline

A

nonpolar, nonaromatic side chains

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6
Q

one of two sulfur containing AA, methyl group attached to sulfur

A

methionine

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7
Q

tryptophan, phenylalanine, and tyrosine

A

aromatic side chains

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8
Q

add an -OH to phenylalanine

A

Tyrosine

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9
Q

serine, threonine, asparagine, glutamine, cysteine

A

Polar side chains

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10
Q

aspartic acid (aspartate) and glutamic acid (glutamate)

A

acidic side chains

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11
Q

arginine, lysine, and histidine

A

basic side chains

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12
Q

Ala (A)

A

Alanine

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13
Q

Arg (R)

A

Arginine

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14
Q

Asn (N)

A

Asparagine

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15
Q

Asp (D)

A

Aspartic acid

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16
Q

Cys (C)

A

Cysteine

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17
Q

Glu (E)

A

Glutamic acid

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18
Q

Gln (Q)

A

Glutamine

19
Q

Gly (G)

A

Glycine

20
Q

His (H)

A

Histidine

21
Q

Ile (I)

A

Isoleucine

22
Q

Leu (L)

A

Leucine

23
Q

Met (M)

A

Methionine

24
Q

Phe (F)

A

Phenylalanine

25
Q

Pro (P)

A

Proline

26
Q

Ser (S)

A

Serine

27
Q

Thr (T)

A

Threonine

28
Q

Trp (W)

A

Tryptophan

29
Q

Tyr (Y)

A

Tyrosine

30
Q

Val (V)

A

Valine

31
Q

Lys (K)

A

Lysine

32
Q

can either accept a proton or donate a proton: how they react depends on the pH of their environment

A

amphoteric species

33
Q

a majority of the species will be protonated

A

pH < pKa

34
Q

a majority of the species will be deprotonated

A

pH > pKa

35
Q

solution acts as a buffer

A

pH of solution id approximately equal to pKa

36
Q

calculated as the average of two nearest pKa values

point at which every molecule is electrically neutral

A

pI isolectric point

37
Q

peptide bond formation is an example of

A

condensation/dehydration reaction

38
Q

linear arrangement of amino acids coded in an organism’s DNA, stabilized by the formation of covalent peptide bonds between adjacent AA

A

primary structure of protein

39
Q

two main structures are alpha-helices and beta-pleated sheets, stabilized by intramolecular hydrogen bonding

A

secondary structure

40
Q

stabilized by intramolecular hydrogen bonding between carbonyl oxygen and amide hydrogen atom four residues down

A

alpha-helix

41
Q

intramolecular hydrogen bonding between carbonyl oxygen atoms on one chain and amide hydrogen atoms in adjacent cahin

A

beta-pleated sheet

42
Q

mostly determined by hydrophillic and hydrophobic interactions between R groups of AA

A

tertiary structure of protein

43
Q

important component of tertiary structure and creates loops in protein chain

A

disulfide bonds

44
Q

proteins that contain more than one polypeptide chain

A

quarternary structure