Effect of External Electric Field Stress on Gliadin Protein Conformation

Proteomes

Ashutosh Singh²  Shirin Munshi¹ 

[1] School of Dietetics and Human Nutrition, McGill University, 21111, Rue Lakeshore, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada; E-Mail:;Department of Bioresource Engineering, McGill University, 21111, Rue Lakeshore, Ste-Anne-de-Bellevue, QC H9X 3V9, Canada; E-Mail:

关键词: molecular dynamic modeling;    gliadin protein;    root mean square deviation;    radius of gyration;    electric field;    hydrogen bonds;    food processing;   

DOI  :  10.3390/proteomes1020025

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.