A conceptual electrophoresis-mediated protein identification method by frictional coefficient during motion under electrical and magnetic interference

Abstract

Protein Identification (PI) based on conventional Mass Spectrometry (MS) is prone to errors. These errors are a result of the inability to solubilize the protein, interference of detergents, usage of wrong protease enzymes, inability to cleavage of the target protein by proteases, and interference of endogenous or exogenous contaminant molecules and calibrants. Conventional Mass Spectrometric PI is solely based on ionization and mass trajectory of protein in a vacuum. Therefore, it is crucial to develop and modify the existing technique not to be entirely dependent on the ionization and mass of the protein molecule in a vacuum. Other than the mass and an overall electrostatic charge of a protein, characteristic steric hindrance on a protein while travelling through a Polyacrylamide Gel matrix, can be used for accurate identification of proteins in Mass Spectrometry. A concept for a modified Mass Spectrometric method based on a Polyacrylamide Gel platform, to utilize the steric hindrance and friction coefficient of the moving protein under the influence of electric field and magnetic fields is proposed in the article. The theoretical approach of the concept is based on the laws of motion, electrical fields, electromagnetism, and Fleming's Left Hand Rule. In this concept, on a Polyacrylamide Gel platform, in an electric field, protein is accelerated to a constant velocity characteristic of the protein introduced to a magnetic field where the radius of the circular trajectory and ratio of mass and overall surface charge of the accelerated protein is measured. This article directs attention to the modification of Mass Spectrometry to improve reliability and accuracy in protein identification.