Domain analysis of human apotransferrin upon interaction with sodium n-dodecyl sulphate: differential scanning calorimetry and circular dichroism approaches

Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

“…For this purpose, we measured the stability and aggregation rate of lysozyme using different methods including differential scanning calorimetry (DSC). DSC is widely used for the study of thermal protein denaturation, and is the sole method for direct determination of the thermodynamic parameters of proteins [35][36][37][38][39]. Here we demonstrate how ␤-casein with negative charge on its surface can change its chaperone activity toward a target protein with positive charge.…”

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

“…The CD for the helix, beta and random forms determined thus can be conversely used to estimate the secondary structure of any protein with X at several wavelengths for the same equation. The α-helical content (f H ) was estimated from the ellipticity value at 222 nm ([θ ] 222 ) as described as follows [48,49]:…”

Thermodynamics of protein denaturation by sodium dodecyl sulfate

“…The amount of H unf for all subpeaks is generally diminished during the presence of SDS specially for N domains (for more information, see Refs. [33,45]). …”

“…The various instruments and methods used were from our previous reports as follows: isothermal titration calorimetry (ITC) (thermal activity monitor 2277, Thermometric, Sweden) [32]; differential scanning calorimetry (DSC) (Scal-1 microcalorimeter, Russia) [33]; circular dichroism (CD) (JASCO J-715 spectropolarimeter, Japan); spectrophotometry (model Shimadzu-3100 spectrophotometer) and microviscometry (Haake D8 microviscometer Germany) [34]; densitometry (model DMA 58 densitometer, Austria) [34]; equilibrium dialysis [35].…”