The relevance of protein stability for biological function and molecular evolution is widely
recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which …

In the tropical species Carica papaya, the articulated and anastomosing laticifers form a
dense network of vessels displayed in all aerial parts of the plant. Damaging the papaya tree …

The term kinetic stability is used to describe proteins that are trapped in a specific
conformation because of an unusually high-unfolding barrier that results in very slow …

In vitro thermal denaturation experiments suggest that, because of the possibility of
irreversible alterations, thermodynamic stability (ie, a positive value for the unfolding Gibbs …

Current control of gastrointestinal nematodes relies primarily on the use of synthetic drugs
and encounters serious problems of resistance. Oral administration of plant cysteine …

The structural and functional aspects along with equilibrium unfolding of procerain, a
cysteine protease from Calotropis procera, were studied in solution. The energetic …

The thermal denaturation of the dimeric enzyme triosephosphate isomerase (TIM) from
Saccharomyces cerevisiae was studied by spectroscopic and calorimetric methods. At low …

The role of electrostatic interactions in the stability and the folding of the N-terminal domain
of the ribosomal protein L9 (NTL9) was investigated by determining the effects of varying the …

The recombinant sucrose: sucrose 1-fructosyltransferase from Schedonorus arundinaceus
(Sa1-SSTrec) produces short-chainfructooligosaccharides (scFOS). In this work, Sa1 …

A zymogen-derived protein, pepsin, appears to be incapable of folding to the native state
without the presence of the prosegment. To better understand the nature of the irreversible …