Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach

Abstract

The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protein isolate but the higher electric field strength of 3 V/nm significantly affected the protein conformation and solvent accessible surface area. The response of protein isolate to various external field stresses demonstrated that it is necessary to gain insight into protein dynamics under electromagnetic fields in order to be able to develop the techniques utilizing them for food processing and other biological applications.

Effect of thermal and electric field treatment on the conformation of Ara h 6 peanut protein allergen

“…The RMSD is calculated by evaluating the changes in the structure with a reference molecule that is normally the control (not under any external stress) (Budi, Legge, Treutlein, & Yarovsky, 2004). RMSD of the protein can be represented using the following equation (Singh et al, 2013b):…”

“…It is well known that during processing food components undergo several chemical and physical changes; hence protein subjected to external stresses such as thermal, chemical and electrical stresses may lead to conformational changes to the molecular structure (Singh, Orsat, & Raghavan, 2013b). The functional properties of proteins depend on their structure and any change in it may alter the functionality (Singh, Munshi, & Raghavan, 2013a).…”

“…The functional properties of proteins depend on their structure and any change in it may alter the functionality (Singh, Munshi, & Raghavan, 2013a). In recent years several studies have been conducted to understand the impact of processing on protein conformation and its relation to the functional properties (Clare Mills et al, 2009;Davis, Smales, & James, 2001;Mondoulet et al, 2005;Singh, Orsat, & Raghavan, 2012;Singh et al, 2013aSingh et al, , 2013b. Several techniques including Fourier Transformation Infrared Spectroscopy (FTIR), Nuclear Magnetic Resonance Imaging (NMR), X-ray diffraction can be used to study the conformational changes in protein during processing, but these techniques are expensive and can only relate the structure of proteins before and after processing.…”

“…Several techniques including Fourier Transformation Infrared Spectroscopy (FTIR), Nuclear Magnetic Resonance Imaging (NMR), X-ray diffraction can be used to study the conformational changes in protein during processing, but these techniques are expensive and can only relate the structure of proteins before and after processing. To overcome these shortcomings Singh et al (Singh et al, 2013b) applied molecular dynamic (MD) simulation technique to gain insight into protein dynamics under the influence of external static electric field. MD simulation technique is widely used to study the structural and dynamic properties of biomolecules and has been applied in the field of pharmacology and molecular biology for development of accurate and novel drug systems.…”

Influence of the electrohydrodynamic process on the properties of dried button mushroom slices: A differential scanning calorimetry (DSC) study

“…Thus, an order is created as the protein dries and the entropy of the protein molecules reduces (Xue et al, 1999). Singh et al (2013b) reported that under the effect of the nominal electric field strength of 0.002 V/nm and 0.004 V/nm, soybean hydrophobic protein reoriented itself in the direction of the electric field; additionally no considerable effect was observed on the secondary structure and surface properties of the protein. However, under an electric field strength of 3 V/nm, the protein unfolded and nearly all the helical structures were damaged.…”