BCH403 EXAMINATION QUESTIONS
WITH 100% VERIFIED ANSWERS
H-bond stabilizing secondary structure - Answer- between amide H's and carbonyl
oxygens
a-Helix - Answer- • Right handed "corkscrew"
One turn every 0.54 nm = 3.6 residues / turn; 0.15 nm per residue
H-bonds stabilize between - Answer- carbonyl oxygen of residue n and the
amidehydrogen of residue n + 4
Disrups a-Helix - Answer- Proline
Help predict tertiary structure - Answer- a-helix
b-Sheets - Answer- -More extended structure than the a-helix
-H-bonding exists between adjacent b-strands
-Alternate side chains point in opposite directions
-b-sheets may have parallel or antiparallel orientation
b-turns - Answer- • Compact turn; allows for abruptreversal (180o) in direction of the
polypeptide chain within 4 amino acid residues.
• Stabilized by a hydrogen bond between residues n and n + 3
• Proline often found at position 2, glycine at position 3 (X-P-G-)
• Turns are often at "edges" of globular proteins; allows for a change in the direction of
the polypeptide chain
Proline forms - Answer- neither a-Helix of b-Sheet
Glycine disrupts - Answer- Secondary structure
Interactions Stabilizing Tertiary Structure - Answer- • Hydrogen bonds
• Ion pair/salt bridges: e.g., Lys+ Glu-
• van der Waals interactions: weak
• Hydrophobic effect
• Disulfide bonds: covalent (strong) but reversible
strongest force behind protein folding - Answer- Hydrophobic Effect
Serum Albumin - Answer- a protein containing manydisulfide bonds
WITH 100% VERIFIED ANSWERS
H-bond stabilizing secondary structure - Answer- between amide H's and carbonyl
oxygens
a-Helix - Answer- • Right handed "corkscrew"
One turn every 0.54 nm = 3.6 residues / turn; 0.15 nm per residue
H-bonds stabilize between - Answer- carbonyl oxygen of residue n and the
amidehydrogen of residue n + 4
Disrups a-Helix - Answer- Proline
Help predict tertiary structure - Answer- a-helix
b-Sheets - Answer- -More extended structure than the a-helix
-H-bonding exists between adjacent b-strands
-Alternate side chains point in opposite directions
-b-sheets may have parallel or antiparallel orientation
b-turns - Answer- • Compact turn; allows for abruptreversal (180o) in direction of the
polypeptide chain within 4 amino acid residues.
• Stabilized by a hydrogen bond between residues n and n + 3
• Proline often found at position 2, glycine at position 3 (X-P-G-)
• Turns are often at "edges" of globular proteins; allows for a change in the direction of
the polypeptide chain
Proline forms - Answer- neither a-Helix of b-Sheet
Glycine disrupts - Answer- Secondary structure
Interactions Stabilizing Tertiary Structure - Answer- • Hydrogen bonds
• Ion pair/salt bridges: e.g., Lys+ Glu-
• van der Waals interactions: weak
• Hydrophobic effect
• Disulfide bonds: covalent (strong) but reversible
strongest force behind protein folding - Answer- Hydrophobic Effect
Serum Albumin - Answer- a protein containing manydisulfide bonds
