Skip Navigation

This Article
Right arrow FREE Full Text (Print PDF) Freely available
Right arrow FREE Full Text (Screen PDF)
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 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 (15)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Griffiths-Jones, S.
Right arrow Articles by Bateman, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Griffiths-Jones, S.
Right arrow Articles by Bateman, A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Bioinformatics Vol. 18 no. 9 2002
Pages 1243-1249
© 2002 Oxford University Press

The use of structure information to increase alignment accuracy does not aid homologue detection with profile HMMs

Sam Griffiths-Jones 1,* and Alex Bateman 1

1 The Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, UK

Received on November 15, 2001 ; revised on February 18, 2002 ; accepted on March 14, 2002

Motivation: The best quality multiple sequence alignments are generally considered to derive from structural superposition. However, no previous work has studied the relative performance of profile hidden Markov models (HMMs) derived from such alignments. Therefore several alignment methods have been used to generate multiple sequence alignments from 348 structurally aligned families in the HOMSTRAD database. The performance of profile HMMs derived from the structural and sequence-based alignments has been assessed for homologue detection.

Results: The best alignment methods studied here correctly align nearly 80% of residues with respect to structure alignments. Alignment quality and model sensitivity are found to be dependent on average number, length, and identity of sequences in the alignment. The striking conclusion is that, although structural data may improve the quality of multiple sequence alignments, this does not add to the ability of the derived profile HMMs to find sequence homologues.

Supplementary information: A list of HOMSTRAD families used in this study and the corresponding Pfam families is available at http://www.sanger.ac.uk/Users/sgj/alignments/map.html

Contact: sgj{at}sanger.ac.uk

* 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
BioinformaticsHome page
A. Heger, S. Mallick, C. Wilton, and L. Holm
The global trace graph, a novel paradigm for searching protein sequence databases
Bioinformatics, September 15, 2007; 23(18): 2361 - 2367.
[Abstract] [Full Text] [PDF]


Home page
BioinformaticsHome page
J. Cheng and P. Baldi
A machine learning information retrieval approach to protein fold recognition
Bioinformatics, June 15, 2006; 22(12): 1456 - 1463.
[Abstract] [Full Text] [PDF]


Home page
Phil Trans R Soc BHome page
R. L Marsden, J. A.G Ranea, A. Sillero, O. Redfern, C. Yeats, M. Maibaum, D. Lee, S. Addou, G. A Reeves, T. J Dallman, et al.
Exploiting protein structure data to explore the evolution of protein function and biological complexity
Phil Trans R Soc B, March 29, 2006; 361(1467): 425 - 440.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
T. Lassmann and E. L. L. Sonnhammer
Automatic assessment of alignment quality
Nucleic Acids Res., December 16, 2005; 33(22): 7120 - 7128.
[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.