文摘
Conformational changes of human carbonic anhydrase II (HCAIIpwt) adsorbed on silica nanoparticles(with an average diameter of 9 nm) have been investigated using differential scanning calorimetry (DSC),and in some specific cases also using circular dichroism (CD) and intrinsic tryptophan fluorescence. Torelate the observed conformational changes to the denaturation stability and/or chemical properties insolution, two N-terminally truncated variants and two mutants of HCAIIpwt containing specific single sitemutations were also investigated. From the thermal transitions of HCAIIpwt adsorbed to the nanoparticleswe found that this variant forms a state that was distinctly different from both the native and moltenglobule states in solution. No thermal transition at all was observed for any of the other variants adsorbedon nanoparticles. CD and intrinsic tryptophan fluorescence indicate that these variants attain a moltenglobule-like state at the surface.