INVESTIGADORES
BIKIEL Damian Ezequiel
capítulos de libros
Título:
Structure, Dynamics, and Reactivity of Heme-Proteins from the Globin Superfamily Investigated through Computer Simulation
Autor/es:
PAU ARROYO-MAÑEZ; LEONARDO BOECHI; DAMIÁN E. BIKIEL; LUCIANA CAPECE; ALEJANDRO D. NADRA; FLAVIO FORTI; AXEL BIDON-CHANAL; F. JAVIER LUQUE; MARCELO A. MARTÍ; DARÍO A. ESTRIN
Libro:
Hemoglobin: Recent Developments and Topics
Editorial:
Transworld Research Network (TRN)
Referencias:
Año: 2010;
Resumen:
  <!-- @page { size: 21cm 29.7cm; margin: 2cm } P { margin-bottom: 0.21cm } -During the last decades computer simulation has become a very useful tool for obtaining information of biomolecular systems. In this chapter we will explore the molecular basis of structure, dynamics, and reactivity of heme proteins from the globin superfamily by means of computer simulation methods. First, we will show that protein structure and dynamics are both key elements for determining heme protein reactivity using as illustrative examples Myoglobin (Mb), Neuroglobin (Ngb), Mycobacterium tuberculosis truncated hemoglobin N (Mt-trHbN), Cerebratulus lacteus mini hemoglobin (CerHb), soybean leghemoglobin (Lba), Campylobacter jejuni truncated hemoglobin P (Cj-trHbP). Second, we will analyze how the structure and dynamics modulate and determine ligand migration processes by means of multiple steering molecular dynamics and implicit ligand sampling schemes using Mycobacterium tuberculosis truncated hemoglobin N and O (Mt-trHbN and Mt-trHbO), and Bacillus subtilis truncated hemoglobin O (Bs-trHbO) as examples. Specifically, we will present results on the dual migration path associated with the nitric oxide dioxygenation reaction, and a comparative analysis of ligand accessibility in truncated hemoglobins belonging to groups II and III.