| Literature DB >> 15062778 |
Abstract
Understanding how denatured polypeptides self-assemble into correctly folded native protein structures is one of the grand challenges of 21st century science. Cytochrome c refolding has been exhaustively studied with a vast array of triggers and spectroscopic probes. Within the past year, atomically detailed dynamics simulations of this process have appeared as well. This wealth of data provides insights into the conformations and dynamics of diverse parts of the polypeptide at many stages in the refolding reaction. The combination of innovative experiments and powerful computational methods promises to produce a model that reconciles many disparate observations of cytochrome c folding.Entities:
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Year: 2004 PMID： 15062778 DOI： 10.1016/j.cbpa.2004.02.009
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN： 1367-5931 Impact factor: 8.822