Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

Paul R. Carey; Munsok Kim; Peter J. Tonge

doi:10.1117/12.57334

1 May 1991 Time resolution of events in an enzyme's active site at 4 K and 300 K using resonance Raman spectroscopy

Paul R. Carey, Munsok Kim, Peter J. Tonge

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.

Citation Download Citation

Paul R. Carey, Munsok Kim, and 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); https://doi.org/10.1117/12.57334

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available