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

Stefan Richter*, Anne Wenzel, Matthias Stein, Razif R. Gabdoulline, Rebecca C. Wade

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

85 Citations (Scopus)

Abstract

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.

Original languageEnglish
JournalNucleic Acids Research
Volume36
Issue numberWeb Server issue
Pages (from-to)W276-280
ISSN0305-1048
DOIs
Publication statusPublished - 1 Jul 2008

Bibliographical note

Funding Information:
This work was supported by the BMBF Hepatosys programme (grant nos. 0313076 and 0313078C) and the Klaus Tschira Foundation. We thank Nils Semmelrock and Bruno Besson for helping to implement early versions of this software. Funding to pay the Open Access publication charges for this article was provided by EML Research gGmbH.

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