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Effect of External Electric Field Stress on Gliadin Protein Conformation

A molecular dynamic (MD) modeling approach was applied to evaluate the effect of external electric field on gliadin protein structure and surface properties. Static electric field strengths of 0.001 V/nm and 0.002 V/nm induced conformational changes in the protein but had no significant effect on it...

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Detalles Bibliográficos
Autores principales: Singh, Ashutosh, Munshi, Shirin, Raghavan, Vijaya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302742/
https://www.ncbi.nlm.nih.gov/pubmed/28250397
http://dx.doi.org/10.3390/proteomes1020025
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author Singh, Ashutosh
Munshi, Shirin
Raghavan, Vijaya
author_facet Singh, Ashutosh
Munshi, Shirin
Raghavan, Vijaya
author_sort Singh, Ashutosh
collection PubMed
description A molecular dynamic (MD) modeling approach was applied to evaluate the effect of external electric field on gliadin protein structure and surface properties. Static electric field strengths of 0.001 V/nm and 0.002 V/nm induced conformational changes in the protein but had no significant effect on its surface properties. The study of hydrogen bond evolution during the course of simulation revealed that the root mean square deviation, radius of gyration and secondary structure formation, all depend significantly on the number hydrogen bonds formed. This study demonstrated that it is necessary to gain insight into protein dynamics under external electric field stress, in order to develop the novel food processing techniques that can be potentially used to reduce or eradicate food allergens.
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spelling pubmed-53027422017-02-27 Effect of External Electric Field Stress on Gliadin Protein Conformation Singh, Ashutosh Munshi, Shirin Raghavan, Vijaya Proteomes Article A molecular dynamic (MD) modeling approach was applied to evaluate the effect of external electric field on gliadin protein structure and surface properties. Static electric field strengths of 0.001 V/nm and 0.002 V/nm induced conformational changes in the protein but had no significant effect on its surface properties. The study of hydrogen bond evolution during the course of simulation revealed that the root mean square deviation, radius of gyration and secondary structure formation, all depend significantly on the number hydrogen bonds formed. This study demonstrated that it is necessary to gain insight into protein dynamics under external electric field stress, in order to develop the novel food processing techniques that can be potentially used to reduce or eradicate food allergens. MDPI 2013-07-04 /pmc/articles/PMC5302742/ /pubmed/28250397 http://dx.doi.org/10.3390/proteomes1020025 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Singh, Ashutosh
Munshi, Shirin
Raghavan, Vijaya
Effect of External Electric Field Stress on Gliadin Protein Conformation
title Effect of External Electric Field Stress on Gliadin Protein Conformation
title_full Effect of External Electric Field Stress on Gliadin Protein Conformation
title_fullStr Effect of External Electric Field Stress on Gliadin Protein Conformation
title_full_unstemmed Effect of External Electric Field Stress on Gliadin Protein Conformation
title_short Effect of External Electric Field Stress on Gliadin Protein Conformation
title_sort effect of external electric field stress on gliadin protein conformation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302742/
https://www.ncbi.nlm.nih.gov/pubmed/28250397
http://dx.doi.org/10.3390/proteomes1020025
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