INQUIMAE   12526
INSTITUTO DE QUIMICA, FISICA DE LOS MATERIALES, MEDIOAMBIENTE Y ENERGIA
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
High Pressure Reveals Structural Determinants for Globin Hexacoordination: Neuroglobin and Myoglobin cases
Autor/es:
LUCIANA CAPECE; MARCELO A. MARTI; ALEJANDRO D. NADRA; AXEL BIDON-CHANAL; F. JAVIER LUQUE; DARIO A. ESTRIN
Lugar:
St. Simons Island, Georgia, Atlanta, USA
Reunión:
Simposio; 49th Sanibel Symposium; 2009
Institución organizadora:
Quantum Theory Project - University of Florida
Resumen:
<!-- @page { size: 21cm 29.7cm; margin: 2cm } P { margin-bottom: 0.21cm } --> <!-- @page { size: 21cm 29.7cm; margin: 2cm } P { margin-bottom: 0.21cm } --> The influence of pressure on the equilibrium between five (5c) and six-coordination (6c) forms in neuroglobin (Ngb) and myoglobin (Mb) has been examined by means of molecular dynamics (MD) simulations at normal and high pressure. The results show that the main effect of high pressure is to reduce the protein mobility without altering the structure in a significant manner. Moreover, our data suggest that the equilibrium between 5c and 6c states in globins is largely controlled by the structure and dynamics of the C-D region. Finally, in agreement with the available experimental data, the free energy profiles obtained from steered MD for both proteins indicate that high pressure enhances hexacoordination. In Ngb the shift in equilibrium is mainly relate to an increase in the 6c5c transition barrier, whereas in Mb such a shift is primarily due to a destabilization of the 5c state.
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