ABSTRACT
Folding is any process by which the polypeptide initially in a denatured state, for example, its set of conformations as it emerges from the ribosome, assumes the folded native state. Assembly is the process by which individual folded polypeptides associate to form their ultimate oligomeric or polymeric protein. One of the major deficits of standard free energy in the folding of a protein results from the requirement to unsolvate those hydrophilic functional groups destined for the interior. The presence of a cystine in a folded polypeptide makes a contribution to the change in configurational entropy for the isomerization between random coil and native protein. The effects of introducing cystines into other proteins, however, differ significantly from those measured in these observations. In the final folded protein, most of the amido protons are well protected from further exchange by its secondary and tertiary structure.
