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Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry
The backbone bond lengths, bond angles, and planarity of a protein are influenced by the backbone conformation (φ,Ψ), but no tool exists to explore these relationships, leaving this area as a reservoir of untapped information about protein structure and function. The Protein Geometry Database (PGD)...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808862/ https://www.ncbi.nlm.nih.gov/pubmed/19906726 http://dx.doi.org/10.1093/nar/gkp1013 |
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author | Berkholz, Donald S. Krenesky, Peter B. Davidson, John R. Karplus, P. Andrew |
author_facet | Berkholz, Donald S. Krenesky, Peter B. Davidson, John R. Karplus, P. Andrew |
author_sort | Berkholz, Donald S. |
collection | PubMed |
description | The backbone bond lengths, bond angles, and planarity of a protein are influenced by the backbone conformation (φ,Ψ), but no tool exists to explore these relationships, leaving this area as a reservoir of untapped information about protein structure and function. The Protein Geometry Database (PGD) enables biologists to easily and flexibly query information about the conformation alone, the backbone geometry alone, and the relationships between them. The capabilities the PGD provides are valuable for assessing the uniqueness of observed conformational or geometric features in protein structure as well as discovering novel features and principles of protein structure. The PGD server is available at http://pgd.science.oregonstate.edu/ and the data and code underlying it are freely available to use and extend. |
format | Text |
id | pubmed-2808862 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28088622010-01-20 Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry Berkholz, Donald S. Krenesky, Peter B. Davidson, John R. Karplus, P. Andrew Nucleic Acids Res Articles The backbone bond lengths, bond angles, and planarity of a protein are influenced by the backbone conformation (φ,Ψ), but no tool exists to explore these relationships, leaving this area as a reservoir of untapped information about protein structure and function. The Protein Geometry Database (PGD) enables biologists to easily and flexibly query information about the conformation alone, the backbone geometry alone, and the relationships between them. The capabilities the PGD provides are valuable for assessing the uniqueness of observed conformational or geometric features in protein structure as well as discovering novel features and principles of protein structure. The PGD server is available at http://pgd.science.oregonstate.edu/ and the data and code underlying it are freely available to use and extend. Oxford University Press 2010-01 2009-11-11 /pmc/articles/PMC2808862/ /pubmed/19906726 http://dx.doi.org/10.1093/nar/gkp1013 Text en © The Author(s) 2009. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Berkholz, Donald S. Krenesky, Peter B. Davidson, John R. Karplus, P. Andrew Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title | Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title_full | Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title_fullStr | Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title_full_unstemmed | Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title_short | Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
title_sort | protein geometry database: a flexible engine to explore backbone conformations and their relationships to covalent geometry |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2808862/ https://www.ncbi.nlm.nih.gov/pubmed/19906726 http://dx.doi.org/10.1093/nar/gkp1013 |
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