Do Well-Populated Intermediates Represent the Pathway of Protein Folding?
The ultimate value of the amino acid sequence is to predict its active three dimensional structure. Protein folding is known to be dictated by the amino acid sequence alone and occurs spontaneously (Anfinsen, 1973). What remain to be fully understood is the mechanism of this spontaneous process. Despite the accumulated efforts, several fundamental issues concerning the folding mechanism of proteins remain hotly debated. For instance, is protein folding a thermodynamically or kinetically governed event (Barker et al., 1992; Creighton, 1990; Dobson, 1990)? is there a preferred pathway or are there multiple pathways (Creighton, 1990; Harrison and Durbin, 1990; Kim and Baldwin, 1990; Weissman and Kim, 1991)? and what are the interplays of “hydrophobic collapse” and “specific tertiary interaction” in driving and guiding the protein folding (Baldwin, 1989; Dill, 1990)? These controversies are caused primarily by our inadequate understanding of the structure and function of protein folding intermediates.
KeywordsRapid Equilibrium Folding Pathway Iodoacetic Acid Folding Intermediate Bovine Pancreatic Trypsin Inhibitor
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