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The effect of heterogeneous structural diffusion on ligand binding to heme proteins

✍ Scribed by W. Doster; Ch. Holzhey; H. Miesmer; F. Post; R. A. Tahir-Kheli

Publisher: Springer Netherlands
Year: 1990
Tongue: English
Weight: 837 KB
Volume: 17
Category: Article
ISSN: 0092-0606
DOI: 10.1007/bf00386603

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✦ Synopsis

The kinetics of ligand binding to heme proteins studied by flash photolysis display an algebraic time dependence at low temperatures in contrast exponential recombination observed under physiological conditions. This result shows that protein structures should be viewed as a tune average of interconverting microstates which are frozen in at low temperatures. We propose a quasi-onedimensional model of heterogeneous structural diffusion coupled to ligand binding which describes freezing transition as an inherent property of protein fluctuations. The structural hopping rates are derived from a temperature invariant spectrum of activation energies. The model predicts power law kinetics of the form t-p at long times. The exponent b is constant (0.5) at high temperatures but decreases below a critical temperature in the frozen regime. These results are compared to experiments performed with myoglobin and /?-chains of hemoglobin.

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