Skip Navigation

Nucleic Acids Research 2004 32(Web Server Issue):W503-W507; doi:10.1093/nar/gkh413
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (313K) Freely available
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 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 Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Shatsky, M.
Right arrow Articles by Wolfson, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shatsky, M.
Right arrow Articles by Wolfson, H. J.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2004, the authors
Nucleic Acids Research, Vol. 32, Web Server issue © Oxford University Press 2004; all rights reserved

BioInfo3D: a suite of tools for structural bioinformatics

Maxim Shatsky, Oranit Dror, Dina Schneidman-Duhovny, Ruth Nussinov1,2 and Haim J. Wolfson*

School of Computer Science, Raymond and Beverly Sackler Faculty of Exact Sciences and 1 Sackler Institute of Molecular Medicine, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv 69978, Israel and 2 Basic Research Program, SAIC-Frederick, Inc., Laboratory of Experimental and Computational Biology, NCI-Frederick, Building 469, Room 151, Frederick, MD 21702, USA

* To whom correspondence should be addressed. Tel: +972 3 640 8040; Fax: +972 3 640 6476; Email: wolfson{at}cs.tau.ac.il
The publisher or recipient acknowledges right of the U.S. Government to retain a nonexclusive, royalty-free license in and to any copyright covering the article.

Received February 26, 2004; Revised and Accepted April 2, 2004

Here, we describe BioInfo3D, a suite of freely available web services for protein structural analysis. The FlexProt method performs flexible structural alignment of protein molecules. FlexProt simultaneously detects the hinge regions and aligns the rigid subparts of the molecules. It does not require an a priori knowledge of the flexible hinge regions. MultiProt and MASS perform simultaneous comparison of multiple protein structures. PatchDock performs prediction of protein–protein and protein–small molecule interactions. The input to all services is either protein PDB codes or protein structures uploaded to the server. All the services are available at http://bioinfo3d.cs.tau.ac.il.


The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated.


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
Protein Sci.Home page
A. Zen, V. Carnevale, A. M. Lesk, and C. Micheletti
Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families
Protein Sci., May 1, 2008; 17(5): 918 - 929.
[Abstract] [Full Text] [PDF]


Home page
Protein Sci.Home page
T. Kaneko, N. Tanaka, and T. Kumasaka
Crystal structures of RsbQ, a stress-response regulator in Bacillus subtilis
Protein Sci., February 1, 2005; 14(2): 558 - 565.
[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.