Chemical denaturation and thermal denaturation of13-lactoglobulin A (f3 — lgA) in the absenceand presence of various concentrations sugar osmolytes and polyols were measured bymonitoring changes in the absorption coefficients at pH 2.0. It has been observed that AGD°(H20), (Gibbs free energy change in absence of denaturant at 25 °C) of f3-1gA in the presenceof 10% (w/v) Trehalose, Sucrose, Sorb...

the thermal denaturation of α-amylase from bacillus amyloliquefaciens has been investigated in the presence and absence of sodium dodecyl sulphate (sds) over the temperature range (293-373) k in 20 mm sodium phosphate buffer, ph 6.9, using temperature scanning spectroscopy. the presence of sds caused the destabilization of α-amylase resulting in a decrease in the temperature of unfolding with a...

We introduce a simplified protein model where the solvent (water) degrees of freedom appear explicitly (although in an extremely simplified fashion). Using this model we are able to recover the thermodynamic phenomenology of proteins over a wide range of temperatures. In particular we describe both the warm and the cold protein denaturation within a single framework, while addressing important ...

Thermal denaturation of a-Lactalbumin in the absence and presence of various concentrations of sucrose,sorbitol, glucose and galactose as sugar osmolytes were measured by monitoring changes in the absorptions thatcarried out in a Lambd 35 UV-Vis double beam spectrophotometer at pH 6.0. These measurements gave valuesof T., (midpoint of denaturation), AH., (enthalpy change at T.), and ACp (consta...

Protein stability is measured by denaturation: When solvent conditions are changed (e.g., temperature, denaturant concentration, or pH) the protein population switches between thermodynamic states. The resulting denaturation curves have baselines. If the baselines are steep, nonlinear, or incomplete, it becomes difficult to characterize protein denaturation. Baselines arise because the chromoph...

We introduce a simplified protein model where the water degrees of freedom appear explicitly (although in an extremely simplified fashion). Using thismodel we are able to recover both the warm and the cold protein denaturation within a single framework, while addressing important issues about the structure of model proteins.

To investigate the interaction and adsorption of drug and carbon nanotube on human serum albumin, three anti-cancer drugs ([Pd(phen)(R-gly)]NO3, R = methyl, propyl and amyl) with different hydrophobic tails and anticancer activities were selected. These drugs have better anti-tumor activity and less side effects than that known cis-platinum drug. Human serum albumin is also ...

chemical denaturation and thermal denaturation of13-lactoglobulin a (f3 — lga) in the absenceand presence of various concentrations sugar osmolytes and polyols were measured bymonitoring changes in the absorption coefficients at ph 2.0. it has been observed that agd°(h20), (gibbs free energy change in absence of denaturant at 25 °c) of f3-1ga in the presenceof 10% (w/v) trehalose, sucrose, sorb...