Intrinsic viscosity of bovine serum albumin conformers

Viscosity and diffusion: crowding and salt effects in protein solutions

“…For the system with 150 mM added NaCl (red open diamonds), the experimental maximum is represented essentially by a single data point at c p = 1 mg/ml, where η red ≈ 6.5 ml/g, whereas the remaining data points describe a nearly constant plateau value of 4.5 ml/g. This plateau value is in good overall agreement with reported values for η red at low c p , in the range of 3.8 to 4.9 ml/g [69][70][71][72].…”

Rheological behavior of wheat gliadins in 50% (v/v) aqueous propanol

“…Large numbers of native globular proteins have [g] values in the range of 2.5-6.0 ml g À1 (Baniel et al, 1992;Hahn and Aragon, 2006;Kumar et al, 1980;Lee and Tripathi, 2005;Monkos, 1997aMonkos, , 2000Monkos, , 2004Monkos, , 2005aSchwenke et al, 1986;Tanford, 1955). However, salt addition, pH adjustment, and denaturation could increase [g] value, by altering shape or charge of proteins (Bohidar, 1998;Britten and Giroux, 2001;Curvale et al, 2008;Vardhanabhuti and Foegeding, 1999;Wilcox and Swaisgood, 2002), or inducing the formation of asymmetric aggregation (Bohidar, 1998;Lonetti et al, 2004) or random coil-like structure (Batista et al, 2005). Furthermore, proteins unfold and behave as linear random coils (Ahmad and Salahuddin, 1974;Shen, 1976;Tanford et al, 1967;Vardhanabhuti and Foegeding, 1999) in the presence of denaturant and/or reducing agent.…”

Viscometric study of pectin. Effect of temperature on the hydrodynamic properties

“…The viscosity of liquids is highly dependent on temperature and its complex relations [28]. The change of viscosity at different temperatures is commonly calculated with an equation of the Arrhenius form:…”