INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
congresos y reuniones científicas
MD Simulations of the Adsorption Process of Cytochrome C on Self Assembled Monolayers,
M. MARTI; L. BOECHI; D. MURGIDA; F. DOCTOROVICH; ESTRIN, D
Congreso; XXXV Reunión Anual de la Sociedad Argentina de Biofísica; 2006
Sociedad Argentina de Biofísica
Most of the natural reactions of redox proteins occur at or in membranes under completely different conditions as those found in solution. Electrochemical and spectroscopical studies of these proteins are therefore performed with the protein immobilized to self assembled monolayer (SAMS) on electrodes. Many studies of these kind have been performed for cytochrome c (cyt c) adsorbed on carboxyl terminated SAMS. A key issue for interpreting these results under a microscopic point of view is the knowledge of the atomistic structure of the SAMS-protein complex. However, although the protein structure in solution and the SAMS structure may be known, no experimental technique allows the determination of the complex structure. The most relevant and unknown parameter is the relative orientation of the protein on the monolayer. Molecular dynamics (MD) simulations are an excellent option to study the structure and dynamics of biomolecules in solution and membranes. In these work we have analyzed using Multiple steered MD (MSMD) the relevant structures of cytochrome c adsorbed on carboxyl terminated SAMS. The MSMD technique, using Jarzinsky´s inequality, allowed us to determine the relevant complex structures (i.e. those with higher binding energy), and study the binding process. Our results also show that the method can be extended to the study of protein-protein or protein-DNA interactions, or even work as a "flexible docking" method.