Temperature behaviour of viscous flow with proteins

Abstract

The paper presents the results of viscosity determinations on aqueous solutions of different mammalian serum albumins at a wide range of concentrations and at temperatures ranging from 278 K to 318 K. On the basis of these measurements and a modified Arrhenius equation, the functional dependence of the solution activation energy of viscous flow on temperature was established. The analysis of the results obtained shows that the activation energy decreases with increasing temperature according to a square function for solutions, water molecules, and the albumins studied. The rate at which the activation energy decreases with increasing temperature is different for each albumin and mainly depends on its hydrodynamic radius.

Activation Thermodynamics and Concentration Scaling of the Viscosity of Unimeric and Aggregated Poloxamer EO93PO54EO93 in Water

“…Apparent properties have been used widely for the investigation of solute–solvent and solute–solute interactions. Monkos used a model very similar to eq for the viscosity of biopolymers except that he assumed that the activation properties of the biopolymers did not depend on the concentration. For simplicity, the apparent contribution of P317 units to the activation properties for viscous flow will be referred to as apparent activation properties.…”

Analysis of bimodal thermally-induced denaturation of type I collagen extracted from calfskin

“…(a) As general rule, the activation energy of viscous ow for a liquid solution ordinarily decreases with temperature, 104 excepting the cases when their viscosity increases with increasing temperature. The viscosity data of CI solutions clearly follow this ordinary tendency.…”

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form

“…It appears that there are only small differences between the values of activation energy for albumins in solutions outside the pI. As has been shown in our recent paper (Monkos 2011) in this case the activation energy mainly depends on hydrodynamic radius of albumin. The values of the activation energy of albumins in solutions at pI are substantially greater than those obtained in solutions outside the pI.…”

“…The quantities S s and E s are interpreted as the entropy and the activation energy of the process of viscous flow, respectively. The quantity D s , in turn, describes the rate at which the activation energy decreases with increasing temperature (Monkos 2011). Fig.…”