Identification of native protein folds amongst a large number of incorrect models

Autor:	Karl Gottsbacher, Georg Casari, Peter Lackner, Manfred Hendlich, Rosina Froschauer, Hannes Floeckner, Manfred J. Sippl, Sabine Weitckus
Rok vydání:	1990
Předmět:	chemistry.chemical_classification Crystallography Low energy Protein structure chemistry Structural Biology Spatial structure Globular protein Native state Native protein Conformational energy Molecular Biology Amino acid
Zdroj:	Journal of Molecular Biology. 216:167-180
ISSN:	0022-2836
DOI:	10.1016/s0022-2836(05)80068-3
Popis:	We present an approach that is able to detect native folds amongst a large number of non-native conformations. The method is based on the compilation of potentials of mean force of the interactions of the Cβ atoms of all amino acid pairs from a database of known three-dimensional protein structures. These potentials are used to calculate the conformational energy of amino acid sequences in a number of different folds. For a substantial number of proteins we find that the conformational energy of the native state is lowest amongst the alternatives. Exceptions are proteins containing large prosthetic groups, Fe-S clusters or polypeptide chains that do not adopt globular folds. We discuss briefly potential applications in various fields of protein structural research.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8423cb0163c6115cd4d682a7e3c73425 https://doi.org/10.1016/s0022-2836(05)80068-3 Zobrazit plný text záznamu