Conformational changes of human carbonic anhydrase II (HCAII(pwt)) adsorbed
on silica nanoparticles (with an average diameter of 9 Mn) have been inves
tigated using differential scanning calorimetry (DSC), and in some specific
cases also using circular dichroism (CD) and intrinsic tryptophan fluoresc
ence. To relate the observed conformational changes to the denaturation sta
bility and/or chemical properties in solution, two N-terminally truncated v
ariants and two mutants of HCAII(pwt) containing specific single site mutat
ions were also investigated. From the thermal transitions of HCAII(pwt) ads
orbed to the nanoparticles we found that this variant forms a state that wa
s distinctly different from both the native and molten globule states in so
lution. No thermal transition at all was observed for any of the other vari
ants adsorbed on nanoparticles. CD and intrinsic tryptophan fluorescence in
dicate that these variants attain a molten globule-like state at the surfac
e.