1 May 1991 Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy
Author Affiliations +
Proceedings Volume 1403, Laser Applications in Life Sciences; (1991) https://doi.org/10.1117/12.57334
Event: Laser Applications in Life Sciences, 1990, Moscow, Russian Federation
Abstract
Resonance Raman spectra for enzyme-substrate intermediates of the type R(C are reported in solution at 300 K and down to 4 K in ice matrices. Analysis reveals that the overall conformation of the substrate-enzyme bonds in the active site remains the same in the range 300 - 4 K but there are important minor spectral changes. Some of these provide access to information on dynamical fluctuations occurring in the active site. Evidence for closely lying fluctuating protein states driving fluctuations in the structure of the bound substrate is discussed. 2.
© (1991) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Paul R. Carey, Paul R. Carey, Munsok Kim, Munsok Kim, Peter J. Tonge, Peter J. Tonge, "Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy", Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); doi: 10.1117/12.57334; https://doi.org/10.1117/12.57334
PROCEEDINGS
3 PAGES


SHARE
RELATED CONTENT


Back to Top