.... In vitro studies reveal a significant affinity for calnuc towards phosphatidylserine, specifically to its C-terminal region, leading to the formation of ‘molten globule’ conformation. Similar structural changes are observed at acidic pH (pH 4), which demonstrates the role of the acidic microenvironment...

..., is a strong competitive inhibitor of cathepsin L. Crammer is a monomeric molten globule in acidic solution, a condition that is similar to the environment in the lysosome where crammer is probably located. Upon binding to cathepsin L, however, crammer undergoes a molten globule-to-ordered structural...

... not refold in vitro . A molten globule folding intermediate accumulated, whereas the wild-type protein folded and associated into active hexamers. In the present study, we report that autophosphorylation of the protein corrected the folding defect. The phosphorylated S120G mutant NDP kinase, either...

... properties similar to those of molten globules [16,17]. In addition to its anti-aggregation properties, it is also found to protect the activity of some enzymes upon heat- induced inactivation. a-Crystallin has been shown to protect catalase against thermal inactivation [15]. Activities of thermo- labile...