Skip Navigation



Nucleic Acids Research Advance Access published online on April 17, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn181
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (3377K) Freely available
Right arrow Screen PDF (462K) Freely available
Right arrowOA All Versions of this Article:
36/suppl_2/W276    most recent
gkn181v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Richter, S.
Right arrow Articles by Wade, R. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Richter, S.
Right arrow Articles by Wade, R. C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Web Server

webPIPSA: a web server for the comparison of protein interaction properties

Stefan Richter1,*, Anne Wenzel1, Matthias Stein1, Razif R. Gabdoulline1,2 and Rebecca C. Wade1

1Molecular and Cellular Modeling Group, EML Research gGmbH, Schloss-Wolfsbrunnenweg 33, 69118 and 2BIOMS (Center for Modeling and Simulation in the Biosciences), University of Heidelberg, Im Neuenheimer Feld 368, 69120 Heidelberg, Germany

*To whom correspondence should be addressed. Tel: +49 6221 533 279; Fax: +49 6221 533 298; Email: stefan.richter{at}eml-r.villa-bosch.de

Received January 31, 2008. Revised March 19, 2008. Accepted March 28, 2008.

Protein molecular interaction fields are key determinants of protein functionality. PIPSA (Protein Interaction Property Similarity Analysis) is a procedure to compare and analyze protein molecular interaction fields, such as the electrostatic potential. PIPSA may assist in protein functional assignment, classification of proteins, the comparison of binding properties and the estimation of enzyme kinetic parameters. webPIPSA is a web server that enables the use of PIPSA to compare and analyze protein electrostatic potentials. While PIPSA can be run with downloadable software (see http://projects.eml.org/mcm/software/pipsa), webPIPSA extends and simplifies a PIPSA run. This allows non-expert users to perform PIPSA for their protein datasets. With input protein coordinates, the superposition of protein structures, as well as the computation and analysis of electrostatic potentials, is automated. The results are provided as electrostatic similarity matrices from an all-pairwise comparison of the proteins which can be subjected to clustering and visualized as epograms (tree-like diagrams showing electrostatic potential differences) or heat maps. webPIPSA is freely available at: http://pipsa.eml.org.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.