Literature DB >> 8913301

Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses.

N Goldman1, J L Thorne, D T Jones.   

Abstract

Previously proposed methods for protein secondary structure prediction from multiple sequence alignments do not efficiently extract the evolutionary information that these alignments contain. The predictions of these methods are less accurate than they could be, because of their failure to consider explicitly the phylogenetic tree that relates aligned protein sequences. As an alternative, we present a hidden Markov model approach to secondary structure prediction that more fully uses the evolutionary information contained in protein sequence alignments. A representative example is presented, and three experiments are performed that illustrate how the appropriate representation of evolutionary relatedness can improve inferences. We explain why similar improvement can be expected in other secondary structure prediction methods and indeed any comparative sequence analysis method.

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Year:  1996        PMID: 8913301     DOI: 10.1006/jmbi.1996.0569

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  25 in total

1.  A phylogenomic study of DNA repair genes, proteins, and processes.

Authors:  J A Eisen; P C Hanawalt
Journal:  Mutat Res       Date:  1999-12-07       Impact factor: 2.433

2.  Structure-based conformational preferences of amino acids.

Authors:  P Koehl; M Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

Review 3.  Genomic biodiversity, phylogenetics and coevolution in proteins.

Authors:  David D Pollock
Journal:  Appl Bioinformatics       Date:  2002

4.  A comparative method for finding and folding RNA secondary structures within protein-coding regions.

Authors:  Jakob Skou Pedersen; Irmtraud Margret Meyer; Roald Forsberg; Peter Simmonds; Jotun Hein
Journal:  Nucleic Acids Res       Date:  2004-09-24       Impact factor: 16.971

5.  Efficient methods for estimating amino acid replacement rates.

Authors:  Lars Arvestad
Journal:  J Mol Evol       Date:  2006-04-28       Impact factor: 2.395

6.  Ancestral population genomics: the coalescent hidden Markov model approach.

Authors:  Julien Y Dutheil; Ganesh Ganapathy; Asger Hobolth; Thomas Mailund; Marcy K Uyenoyama; Mikkel H Schierup
Journal:  Genetics       Date:  2009-07-06       Impact factor: 4.562

7.  A homology identification method that combines protein sequence and structure information.

Authors:  L Yu; J V White; T F Smith
Journal:  Protein Sci       Date:  1998-12       Impact factor: 6.725

8.  Assessing the impact of secondary structure and solvent accessibility on protein evolution.

Authors:  N Goldman; J L Thorne; D T Jones
Journal:  Genetics       Date:  1998-05       Impact factor: 4.562

9.  Predicting protein secondary structure with probabilistic schemata of evolutionarily derived information.

Authors:  M J Thompson; R A Goldstein
Journal:  Protein Sci       Date:  1997-09       Impact factor: 6.725

10.  Getting started in structural phylogenomics.

Authors:  Kimmen Sjölander
Journal:  PLoS Comput Biol       Date:  2010-01-29       Impact factor: 4.475

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