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11 September 1998 Z .Chemical Physics Letters 294 1998 7986

Summary: 11 September 1998
Z .Chemical Physics Letters 294 1998 79­86
Incoherent control of protein conformational state
Noam Agmon, Evgenii B. Krissinel' 1
Department of Physical Chemistry and the Fritz Haber Research Center, The Hebrew UniÕersity, Jerusalem 91904, Israel
Received 17 January 1998; in final form 11 May 1998
The peaks in the temperature-derivative spectra of horse myoglobin-CO are simulated for two cooling protocols: in the
dark and under illumination. The appropriate Smoluchowski equations for both coolingrpreparation and heatingrmonitoring
steps are solved for parameters previously obtained by fitting the transient isothermal binding kinetics. The qualitative
agreement with experiment suggests that the new peak observed after slow cooling under illumination arises from population
which relaxes in the deoxy state during both cooling and heating steps. The analysis shows how temperature and light allow
one to control the inhomogeneous conformational distribution in myoglobin. q 1998 Elsevier Science B.V. All rights
1. Introduction
In small molecules, carefully designed light-pulses
w xallow to control the coherent quantum state 1 .
Z .Large proteins, like myoglobin Mb , exhibit com-
plex reactivity which depends on the internal confor-
w xmational state 2 . The present work demonstrates


Source: Agmon, Noam - Institute of Chemistry, Hebrew University of Jerusalem


Collections: Chemistry