Biophysical analysis of partially folded state of α-lactalbumin in the presence of cationic and anionic surfactants

Volumetric and calorimetric investigations of molecular interactions in some amino acids and peptides in the combined presence of surfactants and glycine betaine

“…Since HTAB and SDS are widely known to denature the proteins at low concentration [18,19], we considered the minimum post micellar concentration of HTAB (m = 2 Á 10 À3 molÁkg À1 ) and SDS (m = 10 Á 10 À3 molÁkg À1 ) in presence of GB (m = 1.0 molÁkg À1 ), to study the present system comprising amino acids and peptides. Here 'm' represents molality of the solutes.…”

Glycine betaine: A widely reported osmolyte induces differential and selective conformational stability and enhances aggregation in some proteins in the presence of surfactants

“…The far (characteristic negative maxima at 208 and 222 nm for native protein) and near (characteristic negative maxima at 272 nm for native protein) UV CD spectra of α‐LA in presence of 0.10 × 10 −3 mol dm ‐3 HTAB had already been shown to induce molten globule state 31. So we investigated the stabilizing property of GB in presence of 0.10 × 10 ‐3 mol dm ‐3 HTAB at two different pH, 4.0 and 7.0, respectively.…”

Interaction of biocompatible natural rosin-based surfactants with human serum albumin: A biophysical study

“…Since, ΔH is negative and ΔS is positive in both the binding sites. The entropy represents the gain in degrees of freedom of the water molecules resulting from hydrophobic interactions that are released to the sample volume upon binding as well as disruption of hydrogen bonds in water [64]. In the present case, from the small positive values of the entropy obtained, it can be assumed that some amount of hydrophobic interactions exists between the binding of rosin molecules.…”