Abstract
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
Current Protein & Peptide Science
Title: Probing Early Events in Ferrous Cytochrome c Folding with Time- Resolved Natural and Magnetic Circular Dichroism Spectroscopies.
Volume: 10 Issue: 5
Author(s): Eefei Chen, Robert A. Goldbeck and David S. Kliger
Affiliation:
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
Abstract: 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.
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Cite this article as:
Chen Eefei, Goldbeck A. Robert and Kliger S. David, Probing Early Events in Ferrous Cytochrome c Folding with Time- Resolved Natural and Magnetic Circular Dichroism Spectroscopies., Current Protein & Peptide Science 2009; 10 (5) . https://dx.doi.org/10.2174/138920309789352001
DOI https://dx.doi.org/10.2174/138920309789352001 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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