Insights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions.
Structure
; 15(6): 741-9, 2007 Jun.
Article
em En
| MEDLINE
| ID: mdl-17562320
ABSTRACT
For a representative set of 64 nonhomologous proteins, each containing a structure solved by NMR and X-ray crystallography, we analyzed the variations in atomic coordinates between NMR models, the temperature (B) factors measured by X-ray crystallography, and the fluctuation dynamics predicted by the Gaussian network model (GNM). The NMR and X-ray data exhibited a correlation of 0.49. The GNM results, on the other hand, yielded a correlation of 0.59 with X-ray data and a distinctively better correlation (0.75) with NMR data. The higher correlation between GNM and NMR data, compared to that between GNM and X-ray B factors, is shown to arise from the differences in the spectrum of modes accessible in solution and in the crystal environment. Mainly, large-amplitude motions sampled in solution are restricted, if not inaccessible, in the crystalline environment of X-rays. Combined GNM and NMR analysis emerges as a useful tool for assessing protein dynamics.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Cristalografia por Raios X
/
Biologia Computacional
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Ressonância Magnética Nuclear Biomolecular
Tipo de estudo:
Prognostic_studies
/
Risk_factors_studies
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article