Which of the following interactions contributes most in protein folding?
Protein folding: The number of distinct combinations of phi and psi angles specifying potential conformations of even a relatively small-- 15 kDa--polypeptide is unbelievably vast, native conformation is specified in the primary sequence. In nature, protein folding takes place in a more orderly and guided fashion.Protein folding generally occurs a stepwise process. In the first stage, as the newly synthesized polypeptide emerges from the ribosome, sho segments fold into secondary structural units that provide local regions of organized structurethe hydrophobic regions segregate into the interior of the protein away from solvent, forming a "molten globule," a paially folded polypeptideCells employ auxiliary proteins to speed the process of folding and to guide it toward a productive conclusionChaperone proteins paicipate in the folding The hsp70 (70 kDa heat shock protein) family of chaperones binds sho sequences ofhydrophobic amino acids- shielding them from solvent.The hsp60 family of chaperones, sometimes called chaperonins, differ in sequence and structure from hsp70 and its homologs. Hsp60 acts later in the folding process, often together with an hsp70 chaperone. The central cavity of the donut-shaped hsp60 chaperone provides a sheltered environment in which a polypeptide can fold until all hydrophobic regions are buried in its interior, thus preempting any tendency toward aggregation.
Covalent Bond
Ionic interactions
Hydrophobic
Vander waal's interaction
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