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)

19
Q

Gly (G)

20
Q

His (H)

21
Q

Ile (I)

A

Isoleucine

22
Q

Leu (L)

23
Q

Met (M)

A

Methionine

24
Q

Phe (F)

A

Phenylalanine

25
Pro (P)
Proline
26
Ser (S)
Serine
27
Thr (T)
Threonine
28
Trp (W)
Tryptophan
29
Tyr (Y)
Tyrosine
30
Val (V)
Valine
31
Lys (K)
Lysine
32
can either accept a proton or donate a proton: how they react depends on the pH of their environment
amphoteric species
33
a majority of the species will be protonated
pH < pKa
34
a majority of the species will be deprotonated
pH > pKa
35
solution acts as a buffer
pH of solution id approximately equal to pKa
36
calculated as the average of two nearest pKa values | point at which every molecule is electrically neutral
pI isolectric point
37
peptide bond formation is an example of
condensation/dehydration reaction
38
linear arrangement of amino acids coded in an organism's DNA, stabilized by the formation of covalent peptide bonds between adjacent AA
primary structure of protein
39
two main structures are alpha-helices and beta-pleated sheets, stabilized by intramolecular hydrogen bonding
secondary structure
40
stabilized by intramolecular hydrogen bonding between carbonyl oxygen and amide hydrogen atom four residues down
alpha-helix
41
intramolecular hydrogen bonding between carbonyl oxygen atoms on one chain and amide hydrogen atoms in adjacent cahin
beta-pleated sheet
42
mostly determined by hydrophillic and hydrophobic interactions between R groups of AA
tertiary structure of protein
43
important component of tertiary structure and creates loops in protein chain
disulfide bonds
44
proteins that contain more than one polypeptide chain
quarternary structure