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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Average 4.7 of 9 Ratings

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? Tested Concept

QID: 100074
1

The primary structure of the protein

9%

(16/173)

2

Hydrogen bonds between amino acids

62%

(108/173)

3

Covalent peptide bonds between amino acids

9%

(16/173)

4

Ionic bonds between amino acids

6%

(10/173)

5

Disulfide bonds between amino acids

11%

(19/173)

M 4 E

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