correo-e: Xavier.Daura@uab.es
Xavier Daura studied Biological Sciences at the Universitat Autònoma de Barcelona (UAB). In 1996, he obtained a Doctor degree in Biological Sciences by the same university for work performed on the simulation and modelling of metallo-carboxypeptidases and their peptide inhibitors, under the supervision of Profs. F. Xavier Avilés and Enrique Querol. He then moved to the Laboratorium für Physikalische Chemie of ETH Zürich, where he joined the group for Informatikgestützte Chemie leaded by Prof. Wilfred F. van Gunsteren. During his 6-year postdoctoral stay at ETH he worked, primarily, on the study of peptide folding by molecular-dynamics simulation. In 2002 he was appointed Research Professor by the Catalan Institution for Research and Advanced Studies (ICREA) and took this position to the Institute of Biotechnology and Biomedicine (IBB) of the UAB, where he currently leads a group on Computational Biology. Current research interests of his group include the study of polypeptide folding and aggregation by molecular-dynamics simulation and the modelling of protein-peptide interactions and protein segments. Since December 2004 he is vice-director of the IBB.
Áreas de interés:
Biología computacional: Física de estructura y función biomolecular.
Simulaciones por dinámica molecular
Desarrollo de campos de fuerza para simulaciones moleculares
Computación de las diferencias de energía libre obtenidas por simulación
Simulación del plegamiento de péptidos y proteínas
Análisis de interacciones biomoleculares
Análisis de la relación estructura-función en proteínas
Modelaje biomolecular
Diseño de drogas
Conferencia
Simulaciones por mécanica molecular del plegamiento de polipéptidos
Resumen
The simulation of peptide folding with atomic resolution has
evolved spectacularly during the last seven years, that is,
from an absolute skepticism on the capability of classical
molecular-dynamics methodology to reproduce complex
biological phenomena such the folding of even simple
oligopeptides -6 to 15 residues- to the seemingly realistic
representation of the thermodynamics and kinetics of folding
of a rapidly increasing number of polypeptides -over 20
residues-. Four factors permitted this rapid progress: the
breakthrough of a second generation of force fields, a rapid
and steady increase of (commodity) computer performance, a
move from local computational resources to large distributed
clusters and, last but not less important, a decision of
particular groups to spend a large computational effort on
projects that most other groups trusted unrealizable at the
time. In my presentation, I will go over a number of
contributions of our group to the field, mostly related to
the thermodynamic and kinetic characterization of the
unfolded state and to the importance of averaging on the
interpretation of experimental data.