Question

Which of the following is untrue about Hydrophobicity?

(a) The hydrophobic effect plays a dominant role in the folding of proteins

(b) Hydrophobic residues aggregate away from contact with water

(c) Hydrophobic residues aggregate to form hydrophobic cores with more polar residues

(d) Hydrophobic residues form the solvent accessible surface but restrict the solubility of the protein

I got this question during an interview for a job.

The origin of the question is Molecular Complementarity topic in division Predicting the Structure of Protein – Biomolecular Interactions of Bioinformatics

Answer 1

Right answer is (d) Hydrophobic residues form the solvent accessible surface but restrict the solubility of the protein

Easiest explanation: Clearly a hydrophobic interface will drive the formation of protein-protein or protein-ligand interactions. It has been noted that hydrophobicity is fairly common at protein-protein interfaces particularly in homodimers (two identical protein monomers that associate) and oligomeric proteins.