BIO 205 PROTEIN STRUCTURE Flashcards

(31 cards)

1
Q

polypeptides are

A

chains of amino acids linked by peptide bonds

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2
Q

amino acid formula

A
H
             |
H2N -- C -- COOH
             |
            R

R= side-chain group

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3
Q

unique R groups defining..

A

specific amino acids

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4
Q

amino acid at pH 7

A
H
                  |
(+) H3N -- C -- COO (-)
                  |
                 R
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5
Q

formation of a polypeptide via peptide bond

A

pics

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6
Q

condensation of 2 amino acids == dipeptide

A

together by amide linkage

- remove 1 water molecule

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7
Q

Polar amino acids - Hydrophilic/Hydrophobic

A

Hydrophilic

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8
Q

NonPolar amino acids - Hydrophilic/Hydrophobic

A

Hydrophobic

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9
Q

Asparatic acid

A

[Asp]
acidic
neg polar, hydrophilic

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10
Q

Glutamic acid

A

[Glu]
acidic
neg polar, hydrophilic

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11
Q

Arganine

A

[Arg]
basic
pos polar, hydrophilic

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12
Q

Lysine

A

[Lys]
basic
pos polar, hydrophilic

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13
Q

Histidine

A

[His]
basic
pos polar, hydrophilic

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14
Q

Asparagine

A

[Asn]

uncharged polar, hydrophilic

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15
Q

Glutamine

A

[Glu]

uncharged polar, hydrophilic

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16
Q

Serine

A

[Ser]

uncharged polar, hydrophilic

17
Q

Threonine

A

[Thr]

uncharged polar, hydrophilic

18
Q

Tyrosine

A

[Tyr]

uncharged polar, hydrophilic

19
Q

Alanine

A

[Ala]

non polar, hydrophobic

20
Q

Glycine

A

[Gly]
non polar, hydrophobic
SMALLEST ; only H

21
Q

Valine

A

[Val]

non polar, hydrophobic

22
Q

Leucine

A

[Leu]

non polar, hydrophobic

23
Q

Isoleucine

A

[Ile]

non polar, hydrophobic

24
Q

Proline

A

[Pro]

non polar, hydrophobic

25
Phenylalanine
[Phe] | non polar, hydrophobic
26
Methionine
[Met] | non polar, hydrophobic
27
Tryptophan
[Trp] | non polar, hydrophobic
28
Cysteine
[Cys] | non polar, hydrophobic
29
unfolded protein
- disordered, high entropy | - few non covalent (enthalpies) interactions
30
folded protein
- highly ordered, low entropy | - many non covalent interactions
31
forces that determine protein folding into its native 3-D structure
- covalent bonding - hydrogen bonding - van der waals - hydrophobic effects