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Conformation of Human Carbonic Anhydrase II Variants Adsorbed to Silica Nanoparticles

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IFM-Laboratory of Applied Physics and IFM-Department of Chemistry, Linköping University, S-581 83 Linköping, Sweden, Department of Biochemistry, Umeå University, S-901 87 Umeå, Sweden , Department of Thermochemistry, University of Lund, S-221 00 Lund, Sweden, and Department of Cell and Molecular Biology, Interface Biophysics, Göteborg University, S-413 90 Göteborg, Sweden
Cite this: Langmuir 1999, 15, 19, 6395–6399
Publication Date (Web):July 7, 1999
Copyright © 1999 American Chemical Society

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    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. To relate the observed conformational changes to the denaturation stability and/or chemical properties in solution, two N-terminally truncated variants and two mutants of HCAIIpwt containing specific single site mutations were also investigated. From the thermal transitions of HCAIIpwt adsorbed to the nanoparticles we found that this variant forms a state that was distinctly different from both the native and molten globule states in solution. No thermal transition at all was observed for any of the other variants adsorbed on nanoparticles. CD and intrinsic tryptophan fluorescence indicate that these variants attain a molten globule-like state at the surface.

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     Laboratory of Applied Physics, Linköping University.


     Corresponding authors.

     IFM-Department of Chemistry, Linköping University.


     Umeå University.

     University of Lund.

     Göteborg University.

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