Module 3: Protein structure/function Flashcards

1
Q

Primary structure

A

sequence of aa in polypeptide chain

linear, aa joined by peptide bonds

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2
Q

Secondary structure

A

driven primarily by peptide backbone interactions
stabilized by H bonds
alpha helix/beta sheet

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3
Q

Tertiary structure

A

driven primarily by side-chain interactions

fold w hydrophobic side chains sheltered inside

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4
Q

Quaternary structure

A

2 or more chains combine

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5
Q

Amino acid structure

A
COO-
                  |
H3N+\_\_ Calpha \_\_H
                  |
                 R (side chain)
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6
Q

Chirality

A

any molecules whose reflection in a mirror cannot be superimposed
attached: 4 non-identical groups

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7
Q

L-chirality

A

L-aa rotates polarized light to the left

***only glycine achiral

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8
Q

Peptide bond

A

formed by a nucleophilic addition-elimination reaction between the carboxyl and amino groups of adjacent amino acids
rigid, planar bond due to resonance delocalization of e-
not a lot of rotation

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9
Q

N-terminal

A

beginning

amino group

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10
Q

C-terminal

A

end

carboxyl group

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11
Q

Non-polar, aliphatic aa

A

Gly (G), Ala (A), Pro (P), Val (V), Leu (L), Ile (I), Met (M)

  • non polar and hydrophobic
  • Ala, Val, Leu: cluster within pr-, stabilize pr- structures
  • Gly, Ala: ambivalent (can reside anywhere on pr-)
  • Pro: R forms covalent bond w a-amino group, found on pr- surface
  • Met: sulfur containing R group
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12
Q

Polar, uncharged R groups

A

Ser (S), Thr (T), Cys (C), Asn (N), Gln (Q)
- can form HBs w water/ other polar mol
- Ser, Thr: found on pr- surface
OH of serine great nucleophile
- Cys: polar side chain form HBs w water, found on pr- surface, SH group great nucleophile
- Asn, Gln: amide counterparts to Asp/Glu, have nonionizable uncharged polar side chains

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13
Q

Aromatic R groups

A

Phe (F), Tyr (Y), Trp (W)

  • hydrophobic, can absorb UV light at 280nm
  • Phe; most hydrophobic aa
  • Tyr: ionizable group, can form HBs
  • Trp: bulky aa
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14
Q

Negatively charged R groups

A

Asp (D), Glu (E)

  • carry neg charge at pH 7
  • hydrophilic, typically found on pr- surface
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15
Q

Positively charged R groups

A

Lys (K), Arg (R), His (H)

  • basic side chain character, very polar, found on pr- exterior/ substrate binding clefts
  • His: least basic, imidazole ring
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16
Q

Multisubunit proteins

Oligomeric vs protomers

A

2/more polypeptides associated noncovalently
Oligomeric: if at least 2 are identical
Protomers: identical units

17
Q

Simple protein

A

contains only aa resides and no other chemical constituents

18
Q

Conjugate protein

prosthetic group

A

contain permanently associated chemical components in addition to aa
Prosthetic group: non-amino acid part