BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Proteins that facilitate the folding of other proteins are called molecular chaperones. The term “chaperone” was first used by Ron Laskey and his colleagues to describe a protein (nucleoplasmin) that is required for the assembly of nucleosomes from histones and DNA.

Detailed explanation-2: -Chaperones are proteins that guide proteins along the proper pathways for folding. They protect proteins when they are in the process of folding, shielding them from other proteins that might bind and hinder the process.

Detailed explanation-3: -Chaperones help proteins to fold and remain folded under extreme temperatures. They also assist misfolded proteins in unfolding and re-folding correctly.

Detailed explanation-4: -Protein folding is essential for a polypeptide chain to acquire its proper structure and function. Protein folding is assisted by HSP called chaperones. Multimeric complexes that form hollow structures, called chaperonins, also participate in protein folding.

Detailed explanation-5: -Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascent proteins to reach their native fold, protect subunits from heat shock during the assembly of complexes, prevent protein aggregation or mediate targeted unfolding and disassembly.