Skip Navigation

Bioinformatics 2005 21(Suppl 1):i449-i458; doi:10.1093/bioinformatics/bti1008
This Article
Right arrow FREE Full Text (Print PDF) 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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Winstanley, H. F.
Right arrow Articles by Deane, C. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Winstanley, H. F.
Right arrow Articles by Deane, C. M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions{at}oupjournals.org

How old is your fold?

Henry F. Winstanley , Sanne Abeln and Charlotte M. Deane *

Department of Statistics 1 South Parks Road, Oxford OX1 3TG, UK

*To whom correspondence should be addressed.

Motivation: At present there exists no age estimate for the different protein structures found in nature. It has become clear from occurrence studies that different folds arose at different points in evolutionary time. An estimation of the age of different folds would be a starting point for many investigations into protein structure evolution: how we arrived at the set of folds we see today. It would also be a powerful tool in protein structure classification allowing us to reassess the available hierarchical methods and perhaps suggest improvements.

Results: We have created the first relative age estimation technique for protein folds. Our method is based on constructing parsimonious scenarios, which can describe occurrence patterns in a phylogeny of species. The ages presented are shown to be robust to the different trees or data types used for their generation. They show correlations with other previously used protein age estimators, but appear to be far more discriminating than any previously suggested technique. The age estimates given are not absolutes but they already offer intriguing insights, like the very different age patterns of {alpha}/ß folds compared with small folds. The {alpha}/ß folds appear on average to be far older than their small fold counterparts.

Availability: Example trees and additional material are available at http://www.stats.ox.ac.uk/~abeln/foldage

Contact: deane{at}stats.ox.ac.uk

Supplementary information: http://www.stats.ox.ac.uk/~abeln/foldage


Received on January 15, 2005; accepted on March 27, 2005

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
Proc. Natl. Acad. Sci. USAHome page
L. Xie and P. E. Bourne
Detecting evolutionary relationships across existing fold space, using sequence order-independent profile-profile alignments
PNAS, April 8, 2008; 105(14): 5441 - 5446.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
K. Fukami-Kobayashi, Y. Minezaki, Y. Tateno, and K. Nishikawa
A Tree of Life Based on Protein Domain Organizations
Mol. Biol. Evol., May 1, 2007; 24(5): 1181 - 1189.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
I.-G. Choi and S.-H. Kim
Evolution of protein structural classes and protein sequence families
PNAS, September 19, 2006; 103(38): 14056 - 14061.
[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.