Cargando…
MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins
MPlot is a webserver that provides a quick and easy way for structural biologists to analyze, visualize and plot tertiary structure contacts of helical membrane proteins. As input, experimentally determined or computationally modeled protein structures in PDB format are required. The automatic analy...
Autores principales: | , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896131/ https://www.ncbi.nlm.nih.gov/pubmed/20484376 http://dx.doi.org/10.1093/nar/gkq401 |
_version_ | 1782183317337014272 |
---|---|
author | Rose, Alexander Goede, Andrean Hildebrand, Peter W. |
author_facet | Rose, Alexander Goede, Andrean Hildebrand, Peter W. |
author_sort | Rose, Alexander |
collection | PubMed |
description | MPlot is a webserver that provides a quick and easy way for structural biologists to analyze, visualize and plot tertiary structure contacts of helical membrane proteins. As input, experimentally determined or computationally modeled protein structures in PDB format are required. The automatic analysis concatenates in house tools to calculate cut-off dependent van der Waals contacts or crossing angles of transmembrane helices with third party tools to compute main chain or side chain hydrogen bonds or membrane planes. Moreover, MPlot allows new features and tools to be added on a regular basis. For that purpose, MPlot was embedded in a framework that facilitates advanced users to compose new workflows from existing tools, or to substitute intermediate results with results from their (own) tools. The outputs can be viewed online in a Jmol based protein viewer, or via automatically generated scripts in PyMOL. For further illustration, the results can be downloaded as a 2D graph, representing the spatial arrangement of transmembrane helices true to scale. For analysis and statistics, all results can be downloaded as text files that may serve as inputs for or as standard data to validate the output of knowledge based tertiary structure prediction tools. URL: http://proteinformatics.charite.de/mplot/. |
format | Text |
id | pubmed-2896131 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28961312010-07-02 MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins Rose, Alexander Goede, Andrean Hildebrand, Peter W. Nucleic Acids Res Articles MPlot is a webserver that provides a quick and easy way for structural biologists to analyze, visualize and plot tertiary structure contacts of helical membrane proteins. As input, experimentally determined or computationally modeled protein structures in PDB format are required. The automatic analysis concatenates in house tools to calculate cut-off dependent van der Waals contacts or crossing angles of transmembrane helices with third party tools to compute main chain or side chain hydrogen bonds or membrane planes. Moreover, MPlot allows new features and tools to be added on a regular basis. For that purpose, MPlot was embedded in a framework that facilitates advanced users to compose new workflows from existing tools, or to substitute intermediate results with results from their (own) tools. The outputs can be viewed online in a Jmol based protein viewer, or via automatically generated scripts in PyMOL. For further illustration, the results can be downloaded as a 2D graph, representing the spatial arrangement of transmembrane helices true to scale. For analysis and statistics, all results can be downloaded as text files that may serve as inputs for or as standard data to validate the output of knowledge based tertiary structure prediction tools. URL: http://proteinformatics.charite.de/mplot/. Oxford University Press 2010-07-01 2010-05-19 /pmc/articles/PMC2896131/ /pubmed/20484376 http://dx.doi.org/10.1093/nar/gkq401 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 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), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Rose, Alexander Goede, Andrean Hildebrand, Peter W. MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title | MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title_full | MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title_fullStr | MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title_full_unstemmed | MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title_short | MPlot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
title_sort | mplot—a server to analyze and visualize tertiary structure contacts and geometrical features of helical membrane proteins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2896131/ https://www.ncbi.nlm.nih.gov/pubmed/20484376 http://dx.doi.org/10.1093/nar/gkq401 |
work_keys_str_mv | AT rosealexander mplotaservertoanalyzeandvisualizetertiarystructurecontactsandgeometricalfeaturesofhelicalmembraneproteins AT goedeandrean mplotaservertoanalyzeandvisualizetertiarystructurecontactsandgeometricalfeaturesofhelicalmembraneproteins AT hildebrandpeterw mplotaservertoanalyzeandvisualizetertiarystructurecontactsandgeometricalfeaturesofhelicalmembraneproteins |