Proteins generally will tend to aggregate under a variety of environmental conditions in
comparison with small drug molecules. The extent of aggregation is dependent on many …

Thermal denaturation-based methods are becoming increasingly used to characterize
protein stability and interactions. Recent technical advances have made these methods …

Pepsin solutions were exposed to high-intensity pulsed electric field (HIPEF) at 25.2, 30.4
and 35.6 kV/cm for 0–500μs. To inactivate pepsin, there was a critical treatment time at each …

Small heat-shock proteins (sHSPs) are ATP-independent molecular chaperones that interact
with partially unfolded proteins, preventing their aberrant aggregation, thereby exhibiting a …

This review summarizes experimental data illuminating the mechanism of suppression of
heat-induced protein aggregation by α-crystallin, one of the small heat shock proteins. The …

Thermal denaturation and aggregation of UV-irradiated βL-crystallin from eye lenses of
steers have been studied. The data on size-exclusion chromatography and SDS-PAGE …

The investigation into the behavior of ficin, bromelain, papain under thermal conditions
holds both theoretical and practical significance. The production processes of medicines …

The relationship between thermal inactivation and conformational changes of
Yarrowialipolytica lipase has been investigated. The enzyme loses activity over 40° C, with a …

Thermal inactivation of oligomeric enzymes results in complex structural changes. This work
deals with thermal inactivation of a native hexamer, jack bean urease. In order to find the …

Thermal aggregation of aspartate aminotransferase from pig heart mitochondria (mAAT) has
been studied at various temperatures and various protein concentrations by dynamic light …