Protein backbone structure determination using only residual dipolar couplings from one ordering medium

Autor:	M, Andrec, P, Du, R M, Levy
Rok vydání:	2002
Předmět:	Models Molecular Protein Folding Protein Conformation Proteins Databases Protein Peptides Nuclear Magnetic Resonance Biomolecular Ubiquitins Algorithms
Zdroj:	Journal of biomolecular NMR. 21(4)
ISSN:	0925-2738
Popis:	Residual dipolar couplings provide significant structural information for proteins in the solution state, which makes them attractive for the rapid determination of protein folds. Unfortunately, dipolar couplings contain inherent structural ambiguities which make them difficult to use in the absence of additional information. In this paper, we describe an approach to the construction of protein backbone folds using experimental dipolar couplings based on a bounded tree search through a structural database. We filter out false positives via an overlap similarity measure that insists that protein fragments assigned to overlapping regions of the sequence must have self-consistent structures. This allows us to determine a backbone fold (including the correct Calpha-Cbeta bond orientations) using only residual dipolar coupling data obtained from one ordering medium. We demonstrate the applicability of the method using experimental data for ubiquitin.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::87073011ae627512c59de027abb614ef https://pubmed.ncbi.nlm.nih.gov/11824753 Zobrazit plný text záznamu Full text from SpringerLink