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Open AccessArticle

Effect of External Electric Field Stress on Gliadin Protein Conformation

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Department of Bioresource Engineering, McGill University, 21111, Rue Lakeshore, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada
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School of Dietetics and Human Nutrition, McGill University, 21111, Rue Lakeshore, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada
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Author to whom correspondence should be addressed.
Proteomes 2013, 1(2), 25-39; https://doi.org/10.3390/proteomes1020025
Received: 1 May 2013 / Revised: 5 June 2013 / Accepted: 20 June 2013 / Published: 4 July 2013
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. View Full-Text
Keywords: molecular dynamic modeling; gliadin protein; root mean square deviation; radius of gyration; electric field; hydrogen bonds; food processing molecular dynamic modeling; gliadin protein; root mean square deviation; radius of gyration; electric field; hydrogen bonds; food processing
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Singh, A.; Munshi, S.; Raghavan, V. Effect of External Electric Field Stress on Gliadin Protein Conformation. Proteomes 2013, 1, 25-39.

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