13 research outputs found
Functional properties and structural characteristics of phosphorylated pea protein isolate
Purification and structural study of the beta form of human cAMP-dependent protein kinase inhibitor
Fluorescence and FTIR study of the pressure-induced denaturation of bovine pancreas trypsin
Relationship of membrane sidedness to the effects of the lipophosphoglycan of Leishmania donovani on the fusion of influenza virus
Properties of proteins and the glassy matrix in maturation-defective mutant seeds ofArabidopsis thaliana
Oligomerization and structural changes of the pore-forming Pseudomonas aeruginosa cytotoxin
Different structural behaviors evidenced in thaumatin-like proteins: A spectroscopic study
Three proteins belonging to the thaumatin-like proteins family were compared in this study from a structural point of view: zeamatin, a new recently isolated PR-5 from Cassia didymobotrya and the commercial sweet-thaumatin. The former two proteins possess antifungal activities while commercial thaumatin is well known to be a natural sweetener. Intrinsic fluorescence studies have evidenced that the three proteins behave differently in unfolding experiments showing different structural rigidity. All the three proteins are more stable at slight acidic buffers, but sweet-thaumatin has a major tendency to destructurate itself. Similar observations were made from circular dichroism studies where a structural dependence relationship from the pH and the solvent used confirmed a hierarchic scale of stability for the three proteins. These structural differences should be considered to be significant for a functional rol