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Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data

Proteins have many functions and predicting these is still one of the major challenges in theoretical biophysics and bioinformatics. Foremost amongst these functions is the need to fold correctly thereby allowing the other genetically dictated tasks that the protein has to carry out to proceed effic...

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Autor principal: Bywater, Robert P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786192/
https://www.ncbi.nlm.nih.gov/pubmed/26963911
http://dx.doi.org/10.1371/journal.pone.0150769
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author Bywater, Robert P.
author_facet Bywater, Robert P.
author_sort Bywater, Robert P.
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description Proteins have many functions and predicting these is still one of the major challenges in theoretical biophysics and bioinformatics. Foremost amongst these functions is the need to fold correctly thereby allowing the other genetically dictated tasks that the protein has to carry out to proceed efficiently. In this work, some earlier algorithms for predicting protein domain folds are revisited and they are compared with more recently developed methods. In dealing with intractable problems such as fold prediction, when different algorithms show convergence onto the same result there is every reason to take all algorithms into account such that a consensus result can be arrived at. In this work it is shown that the application of different algorithms in protein structure prediction leads to results that do not converge as such but rather they collude in a striking and useful way that has never been considered before.
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spelling pubmed-47861922016-03-23 Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data Bywater, Robert P. PLoS One Research Article Proteins have many functions and predicting these is still one of the major challenges in theoretical biophysics and bioinformatics. Foremost amongst these functions is the need to fold correctly thereby allowing the other genetically dictated tasks that the protein has to carry out to proceed efficiently. In this work, some earlier algorithms for predicting protein domain folds are revisited and they are compared with more recently developed methods. In dealing with intractable problems such as fold prediction, when different algorithms show convergence onto the same result there is every reason to take all algorithms into account such that a consensus result can be arrived at. In this work it is shown that the application of different algorithms in protein structure prediction leads to results that do not converge as such but rather they collude in a striking and useful way that has never been considered before. Public Library of Science 2016-03-10 /pmc/articles/PMC4786192/ /pubmed/26963911 http://dx.doi.org/10.1371/journal.pone.0150769 Text en © 2016 Robert P. Bywater http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Bywater, Robert P.
Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title_full Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title_fullStr Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title_full_unstemmed Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title_short Comparison of Algorithms for Prediction of Protein Structural Features from Evolutionary Data
title_sort comparison of algorithms for prediction of protein structural features from evolutionary data
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786192/
https://www.ncbi.nlm.nih.gov/pubmed/26963911
http://dx.doi.org/10.1371/journal.pone.0150769
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