INVESTIGADORES
MARTIN Osvaldo Antonio
congresos y reuniones científicas
Título:
CheShift 2.0: a Quantum-Mechanical-Derived 13C(alpha) Chemical Shift Server for Protein Structure Validation
Autor/es:
VILA, J.A.; ARNAUTOVA Y.A.; MARTIN O.A.; SCHERAGA H.A.
Lugar:
San Diego
Reunión:
Simposio; 24th Annual Symposium of the Protein Society; 2010
Institución organizadora:
Protein Society (USA)
Resumen:
BACKGROUND: Recently, a server (CheShift)1 has been developed to predict 13C(alpha) chemical shifts of protein structures. It is based on the generation of ~700,000 conformations as a function of the torsional angles for all 20 naturally occurring amino acids. Their 13C(alpha) chemical shifts were computed at the DFT level of theory with a small basis set and extrapolated, with an empirically-determined linear regression formula, to reproduce the values obtained with a larger basis set.OBJECTIVE: We present an upgrade of our CheShift server, version 2.0, which now includes nearest-neighbor corrections due to proline-effects and a pH-dependent computation of the chemical shifts for both tautomers of the histidine residue. A series of applications will demonstrate the improvements of the predicted 13C(alpha) chemical shifts for proteins, with respect to the original 1.0 version.