Open Access. Powered by Scholars. Published by Universities.®

Medicine and Health Sciences Commons

Open Access. Powered by Scholars. Published by Universities.®

University of South Florida

Molecular Medicine Faculty Publications

2007

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

Composition Profiler: A Tool For Discovery And Visualization Of Amino Acid Composition Differences, Vladimir Vacic, Vladimir N. Uversky, A. Keith Dunker, Stefano Lonardi Jan 2007

Composition Profiler: A Tool For Discovery And Visualization Of Amino Acid Composition Differences, Vladimir Vacic, Vladimir N. Uversky, A. Keith Dunker, Stefano Lonardi

Molecular Medicine Faculty Publications

Background: Composition Profiler is a web-based tool for semi-automatic discovery of enrichment or depletion of amino acids, either individually or grouped by their physico-chemical or structural properties.

Results: The program takes two samples of amino acids as input: a query sample and a reference sample. The latter provides a suitable background amino acid distribution, and should be chosen according to the nature of the query sample, for example, a standard protein database (e.g. SwissProt, PDB), a representative sample of proteins from the organism under study, or a group of proteins with a contrasting functional annotation. The results of the analysis …


Disprot: The Database Of Disordered Proteins, Megan D. Sickmeier, Justin A. Hamilton, Tanguy Legall, Vladimir Vacic, Marc S. Cortese, Agnes Tantos, Beata Szabo, Peter Tompa, Jake Chen, Vladimir N. Uversky, Zoran Obradovic, A. Keith Dunker Jan 2007

Disprot: The Database Of Disordered Proteins, Megan D. Sickmeier, Justin A. Hamilton, Tanguy Legall, Vladimir Vacic, Marc S. Cortese, Agnes Tantos, Beata Szabo, Peter Tompa, Jake Chen, Vladimir N. Uversky, Zoran Obradovic, A. Keith Dunker

Molecular Medicine Faculty Publications

The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These …