Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (474K) Freely available
Right arrow Supplementary Material
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (23)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Hiller, K.
Right arrow Articles by Münch, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hiller, K.
Right arrow Articles by Münch, R.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2003, Vol. 31, No. 13 3862-3865
© 2003 Oxford University Press

JVirGel: calculation of virtual two-dimensional protein gels

Karsten Hiller, Max Schobert, Claudia Hundertmark1, Dieter Jahn* and Richard Münch

Institut für Mikrobiologie, Technische Universität Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany 1 Institut für Software, Abteilung Informationssysteme, Technische Universität Braunschweig, Mühlenpfordtstrasse 23, D-38106 Braunschweig, Germany

*To whom correspondence should be addressed. Tel: +49 5313915801; Fax: +49 5313915854; Email: d.jahn{at}tu-bs.de

We developed JVirGel, a collection of tools for the simulation and analysis of proteomics data. The software creates and visualizes virtual two-dimensional (2D) protein gels based on the migration behaviour of proteins in dependence of their theoretical molecular weights in combination with their calculated isoelectric points. The utilization of all proteins of an organism of interest deduced from genes of the corresponding genome project in combination with the elimination of obvious membrane proteins permits the creation of an optimized calculated proteome map. The electrophoretic separation behaviour of single proteins is accessible interactively in a JavaTM applet (small application in a web browser) by selecting a pI/MW range and an electrophoretic timescale of interest. The calculated pattern of protein spots helps to identify unknown proteins and to localize known proteins during experimental proteomics approaches. Differences between the experimentally observed and the calculated migration behaviour of certain proteins provide first indications for potential protein modification events. When possible, the protein spots are directly linked via a mouse click to the public databases SWISS-PROT and PRODORIC. Additionally, we provide tools for the serial calculation and visualization of specific protein properties like pH dependent charge curves and hydrophobicity profiles. These values are helpful for the rational establishment of protein purification procedures. The proteomics tools are available on the World Wide Web at http://prodoric.tu-bs.de/proteomics.php.


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


This article has been cited by other articles:


Home page
Brief BioinformHome page
J. Baumbach, A. Tauch, and S. Rahmann
Towards the integrated analysis, visualization and reconstruction of microbial gene regulatory networks
Brief Bioinform, January 1, 2009; 10(1): 75 - 83.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
D. Paape, C. Lippuner, M. Schmid, R. Ackermann, M. E. Barrios-Llerena, U. Zimny-Arndt, V. Brinkmann, B. Arndt, K. P. Pleissner, P. R. Jungblut, et al.
Transgenic, Fluorescent Leishmania mexicana Allow Direct Analysis of the Proteome of Intracellular Amastigotes
Mol. Cell. Proteomics, September 1, 2008; 7(9): 1688 - 1701.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
M. Marcilla, J. J. Cragnolini, and J. A. Lopez de Castro
Proteasome-independent HLA-B27 Ligands Arise Mainly from Small Basic Proteins
Mol. Cell. Proteomics, May 1, 2007; 6(5): 923 - 938.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
K. Hiller, A. Grote, M. Maneck, R. Munch, and D. Jahn
JVirGel 2.0: computational prediction of proteomes separated via two-dimensional gel electrophoresis under consideration of membrane and secreted proteins
Bioinformatics, October 1, 2006; 22(19): 2441 - 2443.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
M.-J. Han and S. Y. Lee
The Escherichia coli Proteome: Past, Present, and Future Prospects
Microbiol. Mol. Biol. Rev., June 1, 2006; 70(2): 362 - 439.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
O. Drews and A. Gorg
DynaProt 2D: an advanced proteomic database for dynamic online access to proteomes and two-dimensional electrophoresis gels
Nucleic Acids Res., January 1, 2005; 33(suppl_1): D583 - D587.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
K. Hiller, A. Grote, M. Scheer, R. Munch, and D. Jahn
PrediSi: prediction of signal peptides and their cleavage positions
Nucleic Acids Res., July 1, 2004; 32(suppl_2): W375 - W379.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
B. D. Halligan, V. Ruotti, W. Jin, S. Laffoon, S. N. Twigger, and E. A. Dratz
ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels
Nucleic Acids Res., July 1, 2004; 32(suppl_2): W638 - W644.
[Abstract] [Full Text] [PDF]



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.