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Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity

While the genome for a given organism stores the information necessary for the organism to function and flourish it is the proteins that are encoded by the genome that perhaps more than anything else characterize the phenotype for that organism. It is therefore not surprising that one of the many ap...

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Autor principal: Bywater, Robert Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4391790/
https://www.ncbi.nlm.nih.gov/pubmed/25856073
http://dx.doi.org/10.1371/journal.pone.0119306
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author Bywater, Robert Paul
author_facet Bywater, Robert Paul
author_sort Bywater, Robert Paul
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description While the genome for a given organism stores the information necessary for the organism to function and flourish it is the proteins that are encoded by the genome that perhaps more than anything else characterize the phenotype for that organism. It is therefore not surprising that one of the many approaches to understanding and predicting protein folding and properties has come from genomics and more specifically from multiple sequence alignments. In this work I explore ways in which data derived from sequence alignment data can be used to investigate in a predictive way three different aspects of protein structure: secondary structures, inter-residue contacts and the dynamics of switching between different states of the protein. In particular the use of Kolmogorov complexity has identified a novel pathway towards achieving these goals.
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spelling pubmed-43917902015-04-21 Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity Bywater, Robert Paul PLoS One Research Article While the genome for a given organism stores the information necessary for the organism to function and flourish it is the proteins that are encoded by the genome that perhaps more than anything else characterize the phenotype for that organism. It is therefore not surprising that one of the many approaches to understanding and predicting protein folding and properties has come from genomics and more specifically from multiple sequence alignments. In this work I explore ways in which data derived from sequence alignment data can be used to investigate in a predictive way three different aspects of protein structure: secondary structures, inter-residue contacts and the dynamics of switching between different states of the protein. In particular the use of Kolmogorov complexity has identified a novel pathway towards achieving these goals. Public Library of Science 2015-04-09 /pmc/articles/PMC4391790/ /pubmed/25856073 http://dx.doi.org/10.1371/journal.pone.0119306 Text en © 2015 Robert Paul Bywater http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Bywater, Robert Paul
Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title_full Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title_fullStr Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title_full_unstemmed Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title_short Prediction of Protein Structural Features from Sequence Data Based on Shannon Entropy and Kolmogorov Complexity
title_sort prediction of protein structural features from sequence data based on shannon entropy and kolmogorov complexity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4391790/
https://www.ncbi.nlm.nih.gov/pubmed/25856073
http://dx.doi.org/10.1371/journal.pone.0119306
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