Probing kinetic mechanisms of protein function and folding with time-resolved natural and magnetic chiroptical spectroscopies.
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.
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
David S
DS
Kliger
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Eefei
E
Chen
Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA.
Robert A
RA
Goldbeck
D002248:Carbon Monoxide / Q000737:chemistry; D002942:Circular Dichroism; D003576:Electron Transport Complex IV / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008280:Magnetics; D009905:Optical Rotatory Dispersion; D010782:Photolysis; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D011506:Proteins; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV