Complementary analysis of thermal transition multiplicity of hen egg-white lysozyme at low pH using X-ray scattering and scanning calorimetry

Article Abstract:

A new method of small-angle X-ray scattering data analysis for studying multiplicity of structural transition of denaturation processes of proteins is presented. The structural transition derived using the new method, called TMA, compares well with that derived using differential scanning calorimetry (DSC) in the thermal denaturation process of hen egg-white lysozyme (HEWL) at the pH range of 2.4-3.1. Both TMA and DSC methods showed that the thermal structural transition of HEWL is mostly characterized by two different spatial-conformational-state transitions in the intramolecular and tertiary structures.

Proteins, Eggs, Eggs (Food), Calorimetry, Protein denaturation

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Small-angle X-ray scattering and calorimetric studies of thermal conformational change of lysozyme depending on pH

Article Abstract:

Research was conducted to examine the thermal structural transition of lysozyme in the temperatures ranging from 20 to 85 degrees C at pH 1.2, 3.9 and 7.0. Small-angle X-ray scattering and differential scanning calorimetry were used in the experiment while alpha-Lactalbumin was used as control. Results indicate evident differences between the thermal structural transitions of the lysozyme solutions at pH 1.2 and at higher pH (pH 3.9 and 7.0).

Conformational analysis, Synchrotron radiation, Hydrogen-ion concentration, Calorimeters

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Characteristics of AOT microemulsion structure depending on apolar solvents

Article Abstract:

Synchrotron radiation small-angle X-ray scattering experiments have been used to investigate the structural features of AOT-reversed micelles, comparing them with four different apolar solvents dependening on Wo. With rising water content, the three different phases appear successively for all systems.

Micelles

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