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Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach

Membrane proteins, which constitute approximately 20% of most genomes, are poorly tractable targets for experimental structure determination, thus analysis by prediction and modelling makes an important contribution to their on-going study. Membrane proteins form two main classes: alpha helical and...

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Detalles Bibliográficos
Autores principales: Taylor, Paul D, Toseland, Christopher P, Attwood, Teresa K, Flower, Darren R
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891692/
https://www.ncbi.nlm.nih.gov/pubmed/17597896
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author Taylor, Paul D
Toseland, Christopher P
Attwood, Teresa K
Flower, Darren R
author_facet Taylor, Paul D
Toseland, Christopher P
Attwood, Teresa K
Flower, Darren R
author_sort Taylor, Paul D
collection PubMed
description Membrane proteins, which constitute approximately 20% of most genomes, are poorly tractable targets for experimental structure determination, thus analysis by prediction and modelling makes an important contribution to their on-going study. Membrane proteins form two main classes: alpha helical and beta barrel trans-membrane proteins. By using a method based on Bayesian Networks, which provides a flexible and powerful framework for statistical inference, we addressed α-helical topology prediction. This method has accuracies of 77.4% for prokaryotic proteins and 61.4% for eukaryotic proteins. The method described here represents an important advance in the computational determination of membrane protein topology and offers a useful, and complementary, tool for the analysis of membrane proteins for a range of applications.
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spelling pubmed-18916922007-06-27 Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach Taylor, Paul D Toseland, Christopher P Attwood, Teresa K Flower, Darren R Bioinformation Prediction Model Membrane proteins, which constitute approximately 20% of most genomes, are poorly tractable targets for experimental structure determination, thus analysis by prediction and modelling makes an important contribution to their on-going study. Membrane proteins form two main classes: alpha helical and beta barrel trans-membrane proteins. By using a method based on Bayesian Networks, which provides a flexible and powerful framework for statistical inference, we addressed α-helical topology prediction. This method has accuracies of 77.4% for prokaryotic proteins and 61.4% for eukaryotic proteins. The method described here represents an important advance in the computational determination of membrane protein topology and offers a useful, and complementary, tool for the analysis of membrane proteins for a range of applications. Biomedical Informatics Publishing Group 2006-11-14 /pmc/articles/PMC1891692/ /pubmed/17597896 Text en © 2005 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Prediction Model
Taylor, Paul D
Toseland, Christopher P
Attwood, Teresa K
Flower, Darren R
Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title_full Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title_fullStr Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title_full_unstemmed Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title_short Alpha helical trans-membrane proteins: Enhanced prediction using a Bayesian approach
title_sort alpha helical trans-membrane proteins: enhanced prediction using a bayesian approach
topic Prediction Model
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891692/
https://www.ncbi.nlm.nih.gov/pubmed/17597896
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