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

International Journal of Molecular Sciences

David S. Kliger¹  Eefei Chen² 

[1] Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA;

关键词: circular dichroism;    optical rotatory dispersion;    magnetic circular dichroism;    magnetic optical rotatory dispersion;    heme proteins;    cytochrome;    phytochrome;    polarization;    quasi-null;    ligand shuttle;   

DOI  :  10.3390/ijms13010683

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.