HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M500181-MCP200v1 5/2/265    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Csizmók, V. Articles by Tompa, P. Search for Related Content PubMed PubMed Citation Articles by Csizmók, V. Articles by Tompa, P. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 5:265-273, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

A Novel Two-dimensional Electrophoresis Technique for the Identification of Intrinsically Unstructured Proteins^*,S

Veronika Csizmók, Edit Szllsi, Peter Friedrich and Peter Tompa

From the Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1518 Budapest, Hungary

Intrinsically unstructured proteins (IUPs) lack a well defined three-dimensional structure under physiological conditions. They constitute a significant fraction of various proteomes, but only a handful of them have so far been identified. Here we report the development of a two-dimensional electrophoresis technique for their de novo recognition and characterization. This technique consists of the combination of native and 8 M urea electrophoresis of heat-treated proteins where IUPs are expected to run into the diagonal, whereas globular proteins either precipitate upon heat treatment or unfold and run off the diagonal in the second dimension. This behavior was born out by a collection of 10 known IUPs and four globular proteins. By running Escherichia coli and Saccharomyces cerevisiae extracts, several novel IUPs were also identified by mass spectrometric analysis of spots at or near the diagonal. By comparing this novel method to several other techniques, such as the PONDR® predictor, hydrophobicity-net charge plot, CD analysis, and gel filtration chromatography, it was shown to provide dependable global assessment of disorder even in dubious cases. Overall the reproducibility and ease of performance of this technique may promote the proteomic scale recognition and characterization of protein disorder.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. Ivanyi-Nagy, J.-P. Lavergne, C. Gabus, D. Ficheux, and J.-L. Darlix RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae Nucleic Acids Res., February 11, 2008; 36(3): 712 - 725. [Abstract] [Full Text] [PDF]

				P. Tompa, P. Banki, M. Bokor, P. Kamasa, D. Kovacs, G. Lasanda, and K. Tompa Protein-Water and Protein-Buffer Interactions in the Aqueous Solution of an Intrinsically Unstructured Plant Dehydrin: NMR Intensity and DSC Aspects Biophys. J., September 15, 2006; 91(6): 2243 - 2249. [Abstract] [Full Text] [PDF]