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Proceedings Paper

Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy
Author(s): Paul R. Carey; Munsok Kim; Peter J. Tonge
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Paper 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.

Paper Details

Date Published: 1 May 1991
PDF: 3 pages
Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); doi: 10.1117/12.57334
Show Author Affiliations
Paul R. Carey, National Research Council Canada (Canada)
Munsok Kim, National Research Council Canada (Canada)
Peter J. Tonge, National Research Council Canada (Canada)


Published in SPIE Proceedings Vol. 1403:
Laser Applications in Life Sciences
Sergei A. Akhmanov; Marina Yu. Poroshina, Editor(s)

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