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Int. J. Mol. Sci. 2012, 13(1), 683-697; doi:10.3390/ijms13010683

Probing Kinetic Mechanisms of Protein Function and Folding with Time-Resolved Natural and Magnetic Chiroptical Spectroscopies

Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA
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Received: 23 December 2011 / Revised: 5 January 2012 / Accepted: 5 January 2012 / Published: 10 January 2012
(This article belongs to the Special Issue Applications of Circular Dichroism)
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Abstract

Recent and ongoing developments in time-resolved spectroscopy have made it possible to monitor circular dichroism, magnetic circular dichroism, optical rotatory dispersion, and magnetic optical rotatory dispersion with nanosecond time resolution. These techniques have been applied to determine structural changes associated with the function of several proteins as well as to determine the nature of early events in protein folding. These studies have required new approaches in triggering protein reactions as well as the development of time-resolved techniques for polarization spectroscopies with sufficient time resolution and sensitivity to probe protein structural changes. View Full-Text
Keywords: circular dichroism; optical rotatory dispersion; magnetic circular dichroism; magnetic optical rotatory dispersion; heme proteins; cytochrome; phytochrome; polarization; quasi-null; ligand shuttle circular dichroism; optical rotatory dispersion; magnetic circular dichroism; magnetic optical rotatory dispersion; heme proteins; cytochrome; phytochrome; polarization; quasi-null; ligand shuttle
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Kliger, D.S.; Chen, E.; Goldbeck, R.A. Probing Kinetic Mechanisms of Protein Function and Folding with Time-Resolved Natural and Magnetic Chiroptical Spectroscopies. Int. J. Mol. Sci. 2012, 13, 683-697.

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