Nahrung 42 (1998) Nr. 3/4, S. 252–253 © WILEY-VCH Verlag GmbH, D-69451 Weinheim, 1998 0027-769X/98/0304-0252$17.50+.50/0 The Hebrew University of Jerusalem, School of Pharmacy, Department of Pharmaceutical Chemistry and *Department of Pharmacy, Jerusalem, Israel. Correspondence to: Dr. Marina Zemser, The Hebrew University of Jerusalem, School of Pharmacy, Department of Pharmaceutical Chemistry,...

AbstractInteraction of Ni complex(Salen= N, N´-ethylene bis(salicylideneimine)) with hen egg-white lysozyme (HEWL) was studied by absorption spectroscopy, competitive binding study and thermal denaturation study. The protein binding affinity of Ni complex was found to be (3.0×103M−1). The binding plot obtained from the absorption titration data gives a binding constant of 2.4 (± 0.3)×103 M...

The results of a thermodynamic calculation of the excess heat capacity that is based on experimental observations and that incorporates the effects of ligand binding on the two-state, thermal denaturation of a protein are presented. For a protein with a single-binding site on the native species and at subsaturating concentrations of ligand, bimodal or unimodal thermograms were computed merely b...

Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize the...

Trypsin (E.C.3.4.21.4) is a serine protease commonly used in proteomics for digestion of proteins. In the present study, the effect of nano-TiO2 on the conformation and catalytic activity of trypsin were studied. The thermal denaturation of trypsin has been investigated in the presence and absence of nano-TiO2 over the temperature range (293-373 K) at pH 3.0 and 7.25, using temperature scanning...

Cold denaturation is a general property of globular proteins, but it is difficult to directly characterize because the transition temperature of protein cold denaturation, T(c), is often below the freezing point of water. As a result, studies of protein cold denaturation are often facilitated by addition of denaturants, using destabilizing pHs or extremes of pressure, or reverse micelle encapsu...

The denaturation of hemoglobin by salicylate in neutral solution is completely reversible. There is a mobile equilibrium between native and denatured hemoglobin in neutral salicylate solution. The higher the salicylate concentration the greater is the percentage denaturation. When there is a mobile equilibrium between the native and denatured forms of a protein, denaturation is caused by the ad...

Despite several careful experimental analyses, it is not yet clear whether protein cold-denaturation is just a "mirror image" of heat denaturation or whether it shows unique structural and energetic features. Here we report that, for a well-characterized small protein, heat denaturation and cold denaturation show dramatically different experimental energetic patterns. Specifically, while heat d...