Updated: 2/2/2018

Protein Structure

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Evidence
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Topic
  • Overview
    • Peptide bond
      • formation
        • carboxyl group on one amino acid + amino group on another amino acid
          • results in a loss of water
        • bond can be broken (hydrolyzed) with addition of water across the bond
    • Orders of protein shape
      • primary
        • amino acid sequence
        • determined by
          • covalent peptide bonds
      • secondary
        • stable folding of individual protein domains
          • a protein may have combinations of different secondary structures
        • common forms
          • α-helix, β-pleated sheet
        • determined by
          • amino acid-amino acid interactions via hydrogen bonds
      • tertiary
        • shape of protein as a whole which imparts functionality to a protein
          • shape may be disrupted (denatured) with changes in solution
        • common forms
          • globular, fibular
        • determined by
          • h-bonding, hydrophobicity, disulfide bridges, ionic bonds
      • quaternary
        • combination of tertiary sub-units
        • examples
          • α + β subunits in hemoglobin
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Questions (1)

(M1.BC.13.9) An experimental compound added to a protein disrupts both alpha helices as well as beta-pleated sheets. Which of the following has the experimental compound affected?

QID: 100074

The primary structure of the protein

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(17/226)

Hydrogen bonds between amino acids

67%

(152/226)

Covalent peptide bonds between amino acids

9%

(20/226)

Ionic bonds between amino acids

5%

(11/226)

Disulfide bonds between amino acids

9%

(21/226)

M 4 E

Select Answer to see Preferred Response

Evidence (2)
VIDEOS & PODCASTS (1)
EXPERT COMMENTS (4)
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