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Nucleic Acids Research 2004 32(Web Server Issue):W595-W601; doi:10.1093/nar/gkh480
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© 2004, the authors
Nucleic Acids Research, Vol. 32, Web Server issue © Oxford University Press 2004; all rights reserved

JavaProtein Dossier: a novel web-based data visualization tool for comprehensive analysis of protein structure

Goran Neshich*, Walter Rocchia2, Adauto L. Mancini, Michel E. B. Yamagishi, Paula R. Kuser, Renato Fileto, Christian Baudet, Ivan P. Pinto, Arnaldo J. Montagner, Juliana F. Palandrani, Joao N. Krauchenco, Renato C. Torres, Savio Souza, Roberto C. Togawa1 and Roberto H. Higa

Núcleo de Bioinformática Estrutural, Embrapa/Informática Agropecuária, Campinas, Brazil, 1 Laboratório de Bioinformática, Embrapa/Recursos Genéticos e Biotecnologia Brasilia, Brazil and 2 NEST-INFM, Scuola Normale Superiore, Piazza dei Cavalieri 7, I-56126 Pisa, Italy

* To whom correspondence should be addressed at EMBRAPA/CNPTIA, Structural Bioinformatics, Av. Andre Tosselo 209-Barão Geraldo, Campus UNICAMP, Campinas, SP 13083-886, Brazil. Tel: +55 19 3789 5774; Fax: +55 19 3289 9594; Email: neshich{at}cnptia.embrapa.br

Received February 13, 2004; Revised April 15, 2004; Accepted May 4, 2004

JavaProtein Dossier (JPD) is a new concept, database and visualization tool providing one of the largest collections of the physicochemical parameters describing proteins' structure, stability, function and interaction with other macromolecules. By collecting as many descriptors/parameters as possible within a single database, we can achieve a better use of the available data and information. Furthermore, data grouping allows us to generate different parameters with the potential to provide new insights into the sequence–structure–function relationship. In JPD, residue selection can be performed according to multiple criteria. JPD can simultaneously display and analyze all the physicochemical parameters of any pair of structures, using precalculated structural alignments, allowing direct parameter comparison at corresponding amino acid positions among homologous structures. In order to focus on the physicochemical (and consequently pharmacological) profile of proteins, visualization tools (showing the structure and structural parameters) also had to be optimized. Our response to this challenge was the use of Java technology with its exceptional level of interactivity. JPD is freely accessible (within the Gold Sting Suite) at http://sms.cbi.cnptia.embrapa.br, http://mirrors.rcsb.org/SMS, http://trantor.bioc.columbia.edu/SMS and http://www.es.embnet.org/SMS/ (Option: JavaProtein Dossier).


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