ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
We hypothesize a model of protein folding based on the Poincaré recursion argument and a number of experimental results, including CD, nmr, and Raman spectra. Our model considers that protein folding in vivo proceeds through prefolded peptide segments consisting of 3 to 14 amino acid residues. Such segments may fold spontaneously into nativelike microdomains within a biologically feasible time, i.e., in the 10-6-10-1 s time scale. If, due to improper recognition and adjustment of their surfaces, these transiently formed secondary structures are not stabilized by long-range interactions, then the protein species occur within a time- and number-averaged spectrum of populations of transient conformational substates until the final, proper adjustment of the segments takes place. However, if, during protein folding, incorrect disulfide (S-S) bonds are formed, then such unique through-space contacts between the different parts of the polypeptide chain are usually restricted to a minimum. It is postulated that unfolding and refolding processes in vitro, and protein folding in vivo, proceed through variably populated quantized substates. The distribution of these substates depends on a number of molecular interactions between the phase and the hydration spheres surrounding the prefolded surfaces of peptide segments and long-range interactions between these prefolded surfaces.
Additional Material:
3 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360240121
