Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
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 ISI Web of Science
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 Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Valafar, H.
Right arrow Articles by Prestegard, J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Valafar, H.
Right arrow Articles by Prestegard, J. H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics Vol. 19 no. 12 2003
Pages 1549-1555
© 2003 Oxford University Press

Rapid classification of a protein fold family using a statistical analysis of dipolar couplings

Homayoun Valafar 1 and James H. Prestegard 2,*

1 Southeast Collaboratory for Structural Genomics
2 Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602, USA

Received on March 21, 2002 ; revised on May 31, 2002 ; accepted on March 4, 2003

Motivation: One of the primary aims of the structural genomics initiative is the determination of representative structures from each protein fold family. Given this objective, it is important to rapidly identify proteins that belong to a family that is already well populated (so they can be eliminated from further studies), or more importantly identify proteins that represent new families of fold.

Results: A method for rapid classification to a fold family by the statistical analyses of unassigned the 15N–1H residual dipolar couplings is presented. The required NMR data can be quickly acquired and analyzed. Using this method, structure determination efforts can be focused on more unique and interesting structures, and the overall efficiency in the construction of an information-rich library can be increased.

Contact: jpresteg{at}ccrc.uga.edu

* To whom correspondence should be addressed.


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
X. Wang, S. Bansal, M. Jiang, and J. H. Prestegard
RDC-assisted modeling of symmetric protein homo-oligomers
Protein Sci., May 1, 2008; 17(5): 899 - 907.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Zweckstetter, G. Hummer, and A. Bax
Prediction of Charge-Induced Molecular Alignment of Biomolecules Dissolved in Dilute Liquid-Crystalline Phases
Biophys. J., June 1, 2004; 86(6): 3444 - 3460.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
Y. Qu, J.-t. Guo, V. Olman, and Y. Xu
Protein structure prediction using sparse dipolar coupling data
Nucleic Acids Res., January 26, 2004; 32(2): 551 - 561.
[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.