Assessing protein structures with a non-local atomic interaction energy

Détails

ID Serval
serval:BIB_D7161D67741E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Assessing protein structures with a non-local atomic interaction energy
Périodique
Journal of Molecular Biology
Auteur⸱e⸱s
Melo  F., Feytmans  E.
ISSN
0022-2836 (Print)
Statut éditorial
Publié
Date de publication
04/1998
Volume
277
Numéro
5
Pages
1141-52
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Apr 17
Résumé
We describe a new approach, based on the energy of non-local interactions, to assess protein structures. The method uses a very sensitive and accurate atomic mean force potential (AMFP) to calculate the non-local energy profile (NL-profile) of a proteins structure. Several protein models, built using the comparative modeling technique and containing several errors, were evaluated. These models exhibit a good stereochemistry and have been previously checked with different, widely used, methods that failed to detect the errors. The AMFP-derived energy profiles are able to correlate high scores with point errors and misalignments in the models. The point errors are frequently found in loops or regions of structural differences between the template and the target protein. The misalignments are clearly detected with very high scores.The performance of the method was also tested for the assessment of X-ray solved protein structures. In a data set of 143 well solved and non-redundant protein structures, we find that the average energy Z-scores, obtained from AMFP, increase as the resolution decreases. In the case of structures that have already been described as having an unusual stereochemistry, very high Z-scores are obtained. Moreover, energy calculations for some pairs of obsolete and replacement proteins always show higher Z-scores for the obsolete proteins. Finally, two particular cases show the usefulness of the profiles in the assessment of X-ray solved protein structures. First, the NL-profile of a protein structure refined in the incorrect space group has very high scores in several regions. One region has already been described to be out-of-register with the density map of the structure. The NL-profile of the re-refined structure with the correct space group is vastly improved. In the second case, the method is able to accurately point out disordered residues, even if the atoms of these residues do not violate the sum of the van der Waals radii. ANOLEA, the program used to calculate the NL-profile of a protein structure containing one or more chains is accessible through the World Wide Web at: http://www.fundp.ac.be/pub/ANOLEA.html.
Mots-clé
Crystallography, X-Ray Databases, Factual Models, Molecular Protein Folding Proteins/*chemistry Software
Pubmed
Web of science
Création de la notice
28/01/2008 11:03
Dernière modification de la notice
20/08/2019 15:56
Données d'usage