Proteins Flashcards

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1
Q

proteins are..?

A

multipurpose molecule

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2
Q

function of proteins?

A
  • enzymes: pepsin, DNA polymerase
  • structure: keratin, collagen
  • carriers and transport: hemoglobin, aquaporin
  • signals cells: insulin
  • receptors
  • defense: antibodies
  • movement: actin and myosin
  • storage: bean seed protein
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3
Q

structure of proteins?

A
  • monomer: amino acids (20 different)
  • polymer: polypeptide
  • can be one or more polypeptide folded and bonded together
  • large complex molecules
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4
Q

three molecules in the structure of proteins?

A
  • hemoglobin
  • rubisco
  • growth hormones
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5
Q

structure of amino acids?

A
  • central carbon
  • amino group
  • carbonyl group
  • r group, side chain
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6
Q

r group?

A
  • variable group
  • different for each amino acid
  • unique chemical properties to each amino acid
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7
Q

effects of different r groups and why?

A
  • non polar: hydrophobic
  • -why? bc of hydrocarbons
  • polar: charges and hydrophilic
  • -why? bc of oxygen and nitrogen
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8
Q

amino acids can be?

A

H+ donors: acids
OR
H+ acceptors: bases

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9
Q

sulfur containing amino acids..?

A
  • disulfide bridges
  • covalent cross between sulfhydryls
  • stabilizes 3D
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10
Q

peptide bonds?

A
  • covalent between NH2 (amine) and COOH (carboxyl)
  • C-N bond
  • repeated sequence: N-C-C
  • can only grow in one direction
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11
Q

2 amino acids form a polypeptide chain by…?

A

dehydration synthesis

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12
Q

C-N?

A

peptide bond

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13
Q

N-C-C

A

amino acid

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14
Q

protein function and structure?

A

-3D: twisted folded and coiled

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15
Q

primary (1°) structure

A
  • order of amino acids in chain
  • sequencing of amino acids by DNA
  • covalent bonds
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16
Q

secondary structure (2°)

A
  • localized folding along polypeptide
  • H bonds
  • a helix (coil)
  • b pleated sheet (pleated)
17
Q

tertiary structure (3°)

A
  • whole molecule folding
  • interactions between distant amino acids
  • hydrophobic interactions (nonpolar amino acids cluster away from water)
  • h bonds and ionic bonds
  • disulfide bridges (S-H)
18
Q

quaternary structure (4°)

A
  • more than one polypeptide chain bonded together

- hydrophobic interactions, h bonds, ionic bonds and disulfide bridges

19
Q

denaturation

A

-unfolding a protein

20
Q

conditions that disrupt denaturation?

A
  • temp
  • pH
  • salinity
21
Q

denaturation alters which structures?

A

2°, 3°, 4°