Incoherent control of protein conformational state Noam 1998


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    • Author:  by Noam Agmon  Evgenii B. Krissinel  

    • Abstract:  The peaks in the temperature-derivati ve 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 reserved.

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