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Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only

We have outlined here some structural aspects of local flexibility. Important functional properties are related to flexible segments. We try to predict regions that have been shown to exhibit the highest probability of being folded in the equilibrium intermediate or native state and will be protecte...

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Detalles Bibliográficos
Autores principales: Dovidchenko, Nikita V, Galzitskaya, Oxana V
Formato: Texto
Lenguaje:English
Publicado: Bentham Open 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570557/
https://www.ncbi.nlm.nih.gov/pubmed/18949078
http://dx.doi.org/10.2174/1874091X00802010077
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author Dovidchenko, Nikita V
Galzitskaya, Oxana V
author_facet Dovidchenko, Nikita V
Galzitskaya, Oxana V
author_sort Dovidchenko, Nikita V
collection PubMed
description We have outlined here some structural aspects of local flexibility. Important functional properties are related to flexible segments. We try to predict regions that have been shown to exhibit the highest probability of being folded in the equilibrium intermediate or native state and will be protected from hydrogen exchange using amino acid sequence only. Our approach FoldUnfold for the prediction of unstructured regions has been applied to seven different proteins. For 80% of the residues considered in this paper we can predict correctly their status: will they be protected or not from hydrogen exchange. An additional goal of our study is to assess whether properties inferred using the bioinformatics approach are easily applicable to predict behavior of proteins in solution.
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spelling pubmed-25705572008-10-23 Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only Dovidchenko, Nikita V Galzitskaya, Oxana V Open Biochem J Article We have outlined here some structural aspects of local flexibility. Important functional properties are related to flexible segments. We try to predict regions that have been shown to exhibit the highest probability of being folded in the equilibrium intermediate or native state and will be protected from hydrogen exchange using amino acid sequence only. Our approach FoldUnfold for the prediction of unstructured regions has been applied to seven different proteins. For 80% of the residues considered in this paper we can predict correctly their status: will they be protected or not from hydrogen exchange. An additional goal of our study is to assess whether properties inferred using the bioinformatics approach are easily applicable to predict behavior of proteins in solution. Bentham Open 2008-06-03 /pmc/articles/PMC2570557/ /pubmed/18949078 http://dx.doi.org/10.2174/1874091X00802010077 Text en © Dovidchenko and Galzitskaya; Licensee Bentham Open. http://creativecommons.org/licenses/by/2.5/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Dovidchenko, Nikita V
Galzitskaya, Oxana V
Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title_full Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title_fullStr Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title_full_unstemmed Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title_short Prediction of Residue Status to Be Protected or Not Protected From Hy-drogen Exchange Using Amino Acid Sequence Only
title_sort prediction of residue status to be protected or not protected from hy-drogen exchange using amino acid sequence only
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570557/
https://www.ncbi.nlm.nih.gov/pubmed/18949078
http://dx.doi.org/10.2174/1874091X00802010077
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