While most current applications of high pressure (HP) are for inactivating deleterious
enzymes, there is evidence that high pressure can induce stabilization and activation of …

The effects of pressure on protein structure and function can vary dramatically depending on
the magnitude of the pressure, the reaction mechanism (in the case of enzymes), and the …

It has long been known that the application of hydrostatic pressure generally leads to the
unfolding of proteins. Despite a relatively large number of reports in the literature over the …

Although it is now relatively well understood how sequence defines and impacts global
protein stability in specific structural contexts, the question of how sequence modulates the …

The structure of [Cu (aq)] 2+ has been investigated by using full multiple-scattering
theoretical (MXAN) analysis of the copper K-edge X-ray absorption (XAS) spectrum and …

The application of hydrostatic pressure generally leads to protein unfolding, implying, in
accordance with Le Chatelier's principle, that the unfolded state has a smaller molar volume …

This study presents an experimental approach, based on the change of Trp fluorescence
between native and denatured states of proteins, which permits to monitor unfolding …

Tissue transglutaminase (tTG) belongs to a class of enzymes that catalyze a cross-linking
reaction between proteins or peptides. The protein activity is known to be finely tuned by Ca …

Abstract Lecitase® Ultra (LU) was immobilized by adsorption on a macroporous resin and
characterized. Meanwhile, the obtained immobilized lipase LXTE-1000-LU was applied in …

The blue copper protein from Pseudomonas aeruginosa, azurin, immobilized at gold
electrodes through hydrophobic interaction with alkanethiol self-assembled monolayers …