Rajendrakumar Singh

TL;DR: This study has carried out thermal denaturation studies of lysozyme, ribonuclease-A, and apo-α-lactalbumin in the presence of various TMAO concentrations at different pH values above and below the pKa, and it is concluded that near room temperature T MAO destabilizes proteins at pH values below its p Ka, whereas it stabilizesprotein at pHvalues above its pKa.

TL;DR: Thermal denaturation curves of lysozyme and ribonuclease-A and measurements of the far- and near-UV CD spectra suggested that secondary and tertiary structures of both proteins in their native and denatured states are not perturbed on the addition of polyols.

TL;DR: In spite of the differences in the structural nature of the heat- and GdmCl-denatured states of each protein, the extent of stabilization by a polyol is same, and the functional dependence of deltaG(D) of proteins in the presence of polyols on denaturant concentration is linear through the full denaturants concentration range.

TL;DR: A comparison of the conformational and thermodynamic properties of the LiClO4-induced molten globule (MG) state with those induced by other solvent conditions suggests that Li ClO4 induces a unique MG state.

TL;DR: It is shown that if osmolytes are compatible with the functional activity of the protein at a given pH and temperature, they should not significantly perturb this denaturation equilibrium under the same experimental conditions.