Practice Questions

The genetic code in DNA determines the amino acid sequence through transcription and translation.

Branched β-carbon side chains create steric hindrance in α-helices.

Binding of oxygen to one subunit increases affinity of the remaining subunits.

These repetitive sequences allow close packing of antiparallel β-sheets.

The φ (phi) and ψ (psi) angles define backbone conformation in proteins.

The C-peptide connects the A and B chains in proinsulin and is removed to form mature insulin.

Resonance restricts rotation around the peptide bond, making these six atoms coplanar.

Domains are independently folded regions within a single polypeptide and are part of tertiary structure.

The Val-6 substitution creates a hydrophobic patch on deoxyhemoglobin, leading to polymerization and sickling of red blood cells.

The oxidizing environment of the endoplasmic reticulum promotes the formation of disulfide bonds in secreted and membrane proteins.