INCOHERENT CONTROL OF PROTEIN CONFORMATIONAL STATE

The peaks in the temperature-derivative spectra of horse myoglobin-CO are simulated for two cooling protocols: in the dark and under illumin ation. The appropriate Smoluchowski equations for both cooling/prepara tion and heating/monitoring steps an solved for parameters previously obtained by fitting the transient isothermal binding kinetics. The qua litative agreement with experiment suggests that the new peak observed after slow cooling under illumination arises from population which re laxes in the deoxy state during both cooling and heating steps. The an alysis shows how temperature and light allow one to control the inhomo geneous conformational distribution in myoglobin. (C) 1998 Elsevier Sc ience B.V. All rights reserved.