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,...

Andreas Hanke Department of Physics and Astronomy, University of Texas, 80 Fort Brown, Brownsville Abstract While the Watson-Crick double-strand is the thermodynamically stable state of DNA in a wide range of temperature and salt conditions even at physiological conditions local denaturation bubbles may open up spontaneously due to thermal activation. By rising the ambient temperature, titratio...

Thermal denaturation of Euphorbia latex amine oxidase (ELAO) has been studied by enzymatic activity, circular dichroism and differential scanning calorimetry. Thermal denaturation of ELAO is shown to be an irreversible process. Checking the validity of two-state it really describes satisfactorily the thermal denaturation of ELAO. Based on this model we obtain the activation energy, parameter T(...

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...

Concentrated solutions of proteins in acid or alkali may become very viscous on denaturation of the protein and under suitable conditions a moderately viscous solution can be converted by heating into a clear gel. These striking changes in viscosity, although they have been known for a long time, have not been studied in detail in recent years and in general the study of denaturation has been n...

To eludicate the role in conformational stability of Cys residues buried in the interior of a protein, the thermodynamic properties of denaturation of mutant alpha subunit of Escherichia coli tryptophan synthase, in which Ser, Ala, Val or Gly was substituted for each of the three Cys residues, were analyzed using calorimetry. The mutants were less stable than the wild type, indicating that Cys ...

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...

Crystalline soybean trypsin inhibitor protein undergoes denaturation on heating which is reversed on cooling. In the range of temperature of 35 to 50 degrees C. a solution of the protein consists of a mixture of native and denatured forms in equilibrium with each other. The equilibrium is only slowly established and its final value at any temperature is the same whether a heated, denatured solu...

What is the mechanism that determines the denaturation of proteins at low temperatures, which is, by now, recognized as a fundamental property of all proteins? We present experimental evidence that clarifies the role of specific interactions that favor the entrance of water into the hydrophobic core, a mechanism originally proposed by Privalov but never proved experimentally. By using a combina...

The susceptibility to denaturation of myofibrillar protein from chicken muscles was investigated and compared with denaturation of myofibrillar protein from pork. Immediately postmortem, the Pectoralis profundus (white muscle) and the Pubo-ishio femorale (red muscle) of six Arbor Acres chickens were collected. The Semimembranosus (white muscle) and Psoas major (red muscle) of three Yorkshire x ...