Temperature, stability, and the hydrophobic interaction

Temperature dependence of the hydrophobic interaction in protein folding.

Accurate calorimetric data for the thermodynamics of transfer of six liquid hydrocarbons to water have been combined with solubility data to provide a model for the temperature dependence of the hydrophobic interaction in protein folding. The model applies at temperatures for which the change in heat capacity (delta Cp) is constant. The extrapolated value of the temperature (Ts) at which the en...

Hydrophobic Interaction Chromatography

modeling for the design of a Biomimetic chimeric ligand. Application to the puriRcation of bovine heart L-lactate dehydrogenase. Biotechnology and Bioengineering 63: 321}331. Lowe CR (1984) Applications of reactive dyes in biotechnology. In: Wiseman A (ed.) Topics in Enzyme and Fermentation Biotechnology, vol. 9. Chichester: Ellis Horwood. Lowe CR, Burton S, Pearson J, Clonis YD and Stead CV (1...

Hydrophobic Interaction Chromatography.

Most proteins and large polypeptides have hydrophobic regions at their surface. These hydrophobic "patches" are due to the presence of the side chains of hydrophobic or nonpolar amino acids such as phenylalanine, tryptophan, alanine, and methionine. These surface hydrophobic regions are interspersed between more hydrophilic or polar regions and the number, size, and distribution of them is a sp...

Hydrophobic Interaction Chromatography

Hydrophobic effect in the pressure-temperature plane.

The free energy of the hydrophobic hydration and the strength of the solvent-mediated attraction between hydrophobic solute molecules are calculated in the pressure-temperature plane. This is done in the framework of an exactly soluble model that is an extension of the lattice model proposed by Kolomeisky and Widom. The model takes into account both the mechanism of the hydrophobic effect domin...