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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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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. |
format | Online Article Text |
id | pubmed-5302742 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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