Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (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 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 (19)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Goldman, N.
Right arrow Articles by Whelan, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Goldman, N.
Right arrow Articles by Whelan, S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Molecular Biology and Evolution 19:1821-1831 (2002)
© 2002 Society for Molecular Biology and Evolution

A Novel Use of Equilibrium Frequencies in Models of Sequence Evolution

Nick Goldman and Simon Whelan

Department of Zoology, University of Cambridge, U.K

Current mathematical models of amino acid sequence evolution are often applied in variants that match their expected amino acid frequencies to those observed in a data set under analysis. This has been achieved by setting the instantaneous rate of replacement of a residue i by another residue j proportional to the observed frequency of the resulting residue j. We describe a more general method that maintains the match between expected and observed frequencies but permits replacement rates to be proportional to the frequencies of both the replaced and resulting residues, raised to powers other than 1. Analysis of a database of amino acid alignments shows that the description of the evolutionary process in a majority (approximately 70% of 182 alignments) is significantly improved by use of the new method, and a variety of analyses indicate that parameter estimation with the new method is well-behaved. Improved evolutionary models increase our understanding of the process of molecular evolution and are often expected to lead to improved phylogenetic inferences, and so it seems justified to consider our new variants of existing standard models when performing evolutionary analyses of amino acid sequences. Similar methods can be used with nucleotide substitution models, but we have not found these to give corresponding significant improvements to our ability to describe the processes of nucleotide sequence evolution.


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
GeneticsHome page
N. Rodrigue, N. Lartillot, and H. Philippe
Bayesian Comparisons of Codon Substitution Models
Genetics, November 1, 2008; 180(3): 1579 - 1591.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
S. C. Choi, A. Hobolth, D. M. Robinson, H. Kishino, and J. L. Thorne
Quantifying the Impact of Protein Tertiary Structure on Molecular Evolution
Mol. Biol. Evol., August 1, 2007; 24(8): 1769 - 1782.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
C. Kosiol, I. Holmes, and N. Goldman
An Empirical Codon Model for Protein Sequence Evolution
Mol. Biol. Evol., July 1, 2007; 24(7): 1464 - 1479.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
J. H. McDonald
Apparent Trends of Amino Acid Gain and Loss in Protein Evolution Due to Nearly Neutral Variation
Mol. Biol. Evol., February 1, 2006; 23(2): 240 - 244.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
S. Whelan, P. I. W. de Bakker, E. Quevillon, N. Rodriguez, and N. Goldman
PANDIT: an evolution-centric database of protein and associated nucleotide domains with inferred trees
Nucleic Acids Res., January 1, 2006; 34(suppl_1): D327 - D331.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
W. R. Atchley, J. Zhao, A. D. Fernandes, and T. Druke
Solving the protein sequence metric problem
PNAS, May 3, 2005; 102(18): 6395 - 6400.
[Abstract] [Full Text] [PDF]


Home page
Mol Biol EvolHome page
N. Lartillot and H. Philippe
A Bayesian Mixture Model for Across-Site Heterogeneities in the Amino-Acid Replacement Process
Mol. Biol. Evol., June 1, 2004; 21(6): 1095 - 1109.
[Abstract] [Full Text] [PDF]


Home page
Integr. Comp. Biol.Home page
B. S. W. Chang
Ancestral Gene Reconstruction and Synthesis of Ancient Rhodopsins in the Laboratory
Integr. Comp. Biol., August 1, 2003; 43(4): 500 - 507.
[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.