Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 10, Issue 5, Pages 464-475Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920309789352001
Keywords
Secondary structure formation; conformational diffusion; unfolded chains; molten globule; heme misligation; time-resolved spectroscopy; far-UV circular dichroism; magnetic circular dichroism; optical rotatory dispersion; cytochrome c
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Funding
- National Institutes of Health [EB02056]
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R01EB002056] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM038549] Funding Source: NIH RePORTER
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In a 1998 collaboration with Tony Fink, we coupled nanosecond circular dichroism methods (TRCD) with a CO-photolysis system for quickly triggering folding in cytochrome c (cyt c) in order to make the first time-resolved far-UV CD measurement of early secondary structure formation in a protein. The small signal observed in that initial study, similar to 10% of native helicity, became the seed for increasingly robust results from subsequent studies bringing additional natural and magnetic circular polarization dichroism and optical rotatory dispersion detection methods (e.g., TRORD, TRMCD, and TRMORD), coupled to fast photolysis and photoreduction triggers, to the study of early folding events. Nanosecond polarization methods are reviewed here in the context of the range of initiation methods and structure-sensitive probes currently available for fast folding studies. We also review the impact of experimental results from fast polarization studies on questions in folding dynamics such as the possibility of multiple folding pathways implied by energy landscape models, the sequence dependence of ultrafast helix formation, and the simultaneity of chain collapse and secondary structure formation implicit in molten globule models for kinetic folding intermediates.
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