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Proteomes 2013, 1(2), 25-39; doi:10.3390/proteomes1020025
Article

Effect of External Electric Field Stress on Gliadin Protein Conformation

1,* , 2
 and 1
Received: 1 May 2013; in revised form: 5 June 2013 / Accepted: 20 June 2013 / Published: 4 July 2013
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Abstract: 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.
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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Singh, A.; Munshi, S.; Raghavan, V. Effect of External Electric Field Stress on Gliadin Protein Conformation. Proteomes 2013, 1, 25-39.

AMA Style

Singh A, Munshi S, Raghavan V. Effect of External Electric Field Stress on Gliadin Protein Conformation. Proteomes. 2013; 1(2):25-39.

Chicago/Turabian Style

Singh, Ashutosh; Munshi, Shirin; Raghavan, Vijaya. 2013. "Effect of External Electric Field Stress on Gliadin Protein Conformation." Proteomes 1, no. 2: 25-39.

Proteomes EISSN 2227-7382 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert