The characterization of protein-folding ki- netics with increasing chain length under various thermody- namic conditions is addressed using the capillarity picture in which distinct spatial regions of the protein are imagined to be folded or trapped and separated by interfaces. The quan- titative capillarity theory is based on the nucleation theory of first-order transitions and the droplet analysis of glasses and random magnets. The concepts of folding funnels and rugged energy landscapes are shown to be applicable in the large size limit just as for smaller proteins.
展开▼
