LIFE SCIENCE

Detailed explanation-1: -Molecular chaperones facilitate and regulate protein conformational change within cells. This encompasses many fundamental cellular processes: including the correct folding of nascent chains; protein transport and translocation; signal transduction and protein quality control.

Detailed explanation-2: -Chaperones prevent aggregation and incorrect folding by binding to and stabilizing partially or totally unfolded protein polypeptides until the polypeptide chain is fully synthesized. They also ensure the stability of unfolded polypeptide chains as they are transported into the subcellular organelles.

Detailed explanation-3: -That electrostatic interactions play such an important role in chaperone-client binding might seem counterintuitive, since chaperones are known to bind to exposed hydrophobic surface areas of un-or misfolded client proteins.

Detailed explanation-4: -In the cell, this fundamental process is aided by molecular chaperones, which act in preventing protein misfolding and aggregation. How this machinery assists newly synthesized polypeptide chains in navigating the complex folding energy landscape is now being understood in considerable detail.