Improving the quality of protein structures derived by NMR spectroscopy.
J Biomol NMR
; 22(3): 281-9, 2002 Mar.
Article
en En
| MEDLINE
| ID: mdl-11991356
Biomolecular structures provide the basis for many studies in several research areas such as homology modelling, structure-based drug design and functional genomics. It is an important prerequisite that the structure is reliable in terms of accurate description of the experimental data, and in terms of good quality of local- and overall geometry. Recent surveys indicate that structures solved by NMR-spectroscopy normally are of lower precision than high-resolution X-ray structures. Here, we present a refinement protocol that improves the quality of protein structures determined by NMR-spectroscopy to the level of those determined by high resolution X-ray crystallography in terms of local geometry. The protocol was tested on experimental data of the proteins IL4 and Ubiquitin and on simulated data of the protein Crambin. In almost all aspects, the protocol yielded better results in terms of accuracy and precision. Independent validation of the results for Ubiquitin, using residual dipolar couplings, indicates that the ensemble of NMR structure is substantially improved by the protocol.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Resonancia Magnética Nuclear Biomolecular
Tipo de estudio:
Evaluation_studies
/
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
J Biomol NMR
Asunto de la revista:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Año:
2002
Tipo del documento:
Article
País de afiliación:
Países Bajos
Pais de publicación:
Países Bajos