BIOMOLECULES AND ENZYMES

Detailed explanation-1: -Chaperonins are chaperone proteins that ensure that other proteins are folded properly. They have two subunits; the larger subunit forms a chamber and the smaller subunit forms the lid. The larger subunit binds misfolded proteins.

Detailed explanation-2: -Molecular chaperones contribute to protein quality control by facilitating the refolding of misfolded polypeptides, interfering directly with protein aggregation, or directing misfolded or aggregated polypeptides to cellular clearance pathways (e.g., ubiquitin-proteasome pathway (UPP), lysosomal autophagy).

Detailed explanation-3: -Chaperones are a functionally related group of proteins assisting protein folding in the cell under physiological and stress conditions. They share the ability to recognize and bind nonnative proteins thus preventing unspecific aggregation.

Detailed explanation-4: -The primary structure of a protein-its amino acid sequence-drives the folding and intramolecular bonding of the linear amino acid chain, which ultimately determines the protein’s unique three-dimensional shape.

Detailed explanation-5: -Protein folding is a very sensitive process that is influenced by several external factors including electric and magnetic fields, temperature, pH, chemicals, space limitation and molecular crowding. These factors influence the ability of proteins to fold into their correct functional forms.