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Current Protein & Peptide Science


ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Probing Early Events in Ferrous Cytochrome c Folding with Time- Resolved Natural and Magnetic Circular Dichroism Spectroscopies.

Author(s): Eefei Chen, Robert A. Goldbeck and David S. Kliger

Volume 10, Issue 5, 2009

Page: [464 - 475] Pages: 12

DOI: 10.2174/138920309789352001

Price: $65


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, ∼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 structuresensitive 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.

Keywords: Secondary structure formation, conformational diffusion, unfolded chains, molten globule, heme misligation, timeresolved spectroscopy, far-UV circular dichroism, magnetic circular dichroism, optical rotatory dispersion, cytochrome c

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