Comparison of the conformational stability of the non-native α-helical intermediate of thiol-modified β-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH

Identification of cow and buffalo milk based on Beta carotene and vitamin-A concentration using fluorescence spectroscopy

“…Synchronous fluorescence is a complex pattern for the reason that the emission monochromator collects fluorescent emission only when the absorption and emission bands of a biomolecule overlap by the specified wavelength interval ‘Δλ’ [3, 35]. Fig 3 depicts the front face synchronous fluorescence emission intensity results as a function of wavelength interval and excitation wavelength.…”

“…The most important nutritious components of milk are proteins, carbohydrate, vitamins and fats [1]. Among all proteins, Beta-lactoglobulin (β-lg) is a major protein that exists at the normal pH of bovine milk which account for approximately 10–15% of total milk proteins and about 60% of whey protein [2, 3]. Apart from other essential elements, milk is a rich source of carotenoids.…”

Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: Spectroscopic and calorimetric approaches

“…In the presence of salts, these acid-unfolded states acquire compactness similar to the molten globule state and exhibit higher stability [6,11]. Salts, at moderate concentrations, play a vital role in the electrostatic screening of the repulsive forces and in the hydrophobic interactions at very low and very high pH [12,[34][35][36].…”

The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity

“…However, studies of the detergent association with membrane proteins using CD, fluorescence and calorimetric techniques have suggested the importance of the detergent in the stabilization of the protein under non-native condition [48,49], suggesting that the stability of the solubilized protein structure depends on the detergent/protein ratio.…”