Skip Navigation



Bioinformatics Advance Access published online on October 4, 2006
Bioinformatics, doi:10.1093/bioinformatics/btl504
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
22/23/2948    most recent
btl504v1
Right arrow Comments: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when Comments are posted
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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Galzitskaya, O. V.
Right arrow Articles by Lobanov, M. YU.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Galzitskaya, O. V.
Right arrow Articles by Lobanov, M. YU.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author (2006). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received July 12, 2006
Revised August 29, 2006
Accepted September 22, 2006

Applications note

FoldUnfold: web server for the prediction of disordered regions in protein chain

Oxana V. Galzitskaya 1 *, Sergiy O. Garbuzynskiy 1, and Michail YU. Lobanov 1

1 Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

* To whom correspondence should be addressed.
Oxana V. Galzitskaya, E-mail: ogalzit{at}vega.protres.ru


  Abstract

Summary: Identification of disordered regions in polypeptide chains is very important because such regions are essential for protein function. A new parameter, namely mean packing density of residues has been introduced to detect disordered regions in a protein sequence. We have demonstrated that regions with weak expected packing density would be responsible for the appearance of disordered regions. Our method (FoldUnfold) has been tested on datasets of globular proteins (559 proteins) and long disordered protein segments (129 proteins) and showed improved performance over some other widely used methods, such as DISOPRED, PONDR VL3H, IUPred, GlobPlot.

Availability: The FoldUnfold server is available for users at http://skuld.protres.ru/~mlobanov/ogu/ogu.cgi. There is a link to our server through the web-site of DisProt (http://www.disprot.org/predictors.php).

Associate Editor: Dmitrij Frishman
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
 Nucleic Acids ResHome page
B. W. Brandt, J. Heringa, and J. A. M. Leunissen
SEQATOMS: a web tool for identifying missing regions in PDB in sequence context
Nucleic Acids Res., July 1, 2008; 36(suppl_2): W255 - W259.
[Abstract] [Full Text] [PDF]

Home page
 BioinformaticsHome page
S. Hirose, K. Shimizu, S. Kanai, Y. Kuroda, and T. Noguchi
POODLE-L: a two-level SVM prediction system for reliably predicting long disordered regions
Bioinformatics, August 15, 2007; 23(16): 2046 - 2053.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
C.-T. Su, C.-Y. Chen, and C.-M. Hsu
iPDA: integrated protein disorder analyzer
Nucleic Acids Res., July 13, 2007; 35(suppl_2): W465 - W472.
[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.