Cargando…

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)...

Descripción completa

Detalles Bibliográficos
Autores principales: Berkholz, Donald S., Krenesky, Peter B., Davidson, John R., Karplus, P. Andrew
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2010
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
_version_ 1782176539918467072
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
work_keys_str_mv AT berkholzdonalds proteingeometrydatabaseaflexibleenginetoexplorebackboneconformationsandtheirrelationshipstocovalentgeometry
AT kreneskypeterb proteingeometrydatabaseaflexibleenginetoexplorebackboneconformationsandtheirrelationshipstocovalentgeometry
AT davidsonjohnr proteingeometrydatabaseaflexibleenginetoexplorebackboneconformationsandtheirrelationshipstocovalentgeometry
AT karpluspandrew proteingeometrydatabaseaflexibleenginetoexplorebackboneconformationsandtheirrelationshipstocovalentgeometry