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Protein Science, Vol 7, Issue 11 2301-2313, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Effects of pressure on the structure of metmyoglobin: Molecular dynamics predictions for pressure unfolding through a molten globule intermediate

W. B. FLORIANO, MAC. NASCIMENTO, G. B. DOMONT and W. A. GODDARD-III
Materials and Process Simulation Center, Beckman Institute, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125 Centro de Ciencias Exatas, Departamento de Fisica Universidade Federal do Espirito Santo, Vitoria, ES, 29060-900, Brazil

We investigated the pathway for pressure unfolding of metmyoglobin using molecular dynamics (MD) for a range of pressures (0.1 MPa to 1.2 GPa) and a temperature of 300 K. We find that the unfolding of metmyoglobin proceeds via a two-step mechanism native -> molten globule intermediate -> unfolded, where the molten globule forms at 700 MPa. The simulation describes qualitatively the experimental behavior of metmyoglobin under pressure. We find that unfolding of the alpha-helices follows the sequence of migrating hydrogen bonds (i,i + 4) -> (i,i + 2).
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