Biophysical Behavior and Hydrophobic Interactions of Globular Proteins with Aqueous Binary Solutions
Man SinghChemistry Research Laboratory, Deshbandhu College, University of Delhi, New Delhi - 110 019 (India)
Abstract: Densities (ρ) and viscosities (η) for 0.5 to 2.0 mg %/100 mL aqueous solutions of Bovine Serum Albumin (BSA), Egg Albumin (E Alb), Lysozyme (Lyso), Gram and Soya Bean proteins with 0.5 mg % mL subsequent increment at temperatures from 293.1, 298.1 and 303.1 Kelvin (K) 0.05°C temperatures were obtained. The densities decrease with concentrations and temperatures except BSA, Gram and Soya with stronger structural interactions for BSA at lower temperatures. The viscosities increase with increase in conc. The Gram shows higher densities at 293.1 K with weaker hydrophobic and slightly higher hydrophilic interactions. The viscosities are higher than those of the water and infer entanglement of biopolymer molecules with drag of a solvent flow. So the proteins undergo structural unfolding with aqueous solutions due to a moderately polar (-NH~~CO-) peptide bond of the protein. Each protein showed stronger hydrophobic interactions than hydrophilic Interaction and Gram protein showed maximum densities at 293.1 K.
Keywords: Structure breaking; making; hydrodynamic sphere; Newtonian flow Back to TOC