journal article·1999-09-01

Conformation of Human Carbonic Anhydrase II Variants Adsorbed to Silica Nanoparticles

Peter Billsten, Uno Carlsson, Bengt Harald Jonsson, Gerd Olofsson, Fredrik Höök, Hans Elwing

Langmuir· Volume 15· Issue 19
Publisher page

Abstract

Conformational changes of human carbonic anhydrase II (HCAII pwt ) 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 HCAII pwt containing specific single site mutations were also investigated. From the thermal transitions of HCAII pwt 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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Research context

OpenAlex topics: Enzyme function and inhibition · Cholinesterase and Neurodegenerative Diseases · Chemical Reaction Mechanisms

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

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

References (26)

Show source-provided references
1. Norde, W.; Haynes, C. A. Reversibility and Mechanism of Protein Adsorption InProteins at Interfaces II; Horbett, T. J., Brash, J. L., Eds.; ACS Symposium Series 602, American Chemical Society: Washington, DC, 1995; pp 26−39.10.1021/bk-1995-0602.ch002 ↗
2. Marco M. · Meas. Sci. Technol. · 1996 · 7 · 154710.1088/0957-0233/7/11/002 ↗
3. Proteins · 1995
4. Håkansson K. · J. Mol. Biol. · 1992 · 227 · 119210.1016/0022-2836(92)90531-N ↗
5. Andersson D. · Biochemistry · 1997 · 36 · 462310.1021/bi961925n ↗
6. Aronsson G. · Biochemistry · 1995 · 34 · 215310.1021/bi00007a008 ↗
7. Carlsson U. · Curr. Opin. Struct. Biol. · 1995 · 5 · 48210.1016/0959-440X(95)80032-8 ↗
8. Freskgård P.-O. · FEBS Lett. · 1991 · 289 · 11710.1016/0014-5793(91)80922-P ↗
9. Mårtensson L.-G. · Biochemistry · 1993 · 3 · 22410.1021/bi00052a029 ↗
10. Kuwajima, K.Proteins: Struct., Funct., Genet.1989,6, 87.10.1002/prot.340060202 ↗
11. Billsten P. · FEBS Lett. · 1997 · 402 · 6710.1016/S0014-5793(96)01431-7 ↗
12. Buijs J. · J. Colloid Interface Sci. · 1997 · 190 · 17110.1006/jcis.1997.4876 ↗
13. McGuire J. · J. Colloid Interface Sci. · 1995 · 170 · 18210.1006/jcis.1995.1087 ↗
14. McGuire J. · J. Colloid Interface Sci. · 1995 · 170 · 19310.1006/jcis.1995.1088 ↗
15. Lindgren M. · J. Chem. Soc., Perkin Trans. 2 · 1993 · 200310.1039/P29930002003 ↗
16. Svensson M. · Biochemistry · 1995 · 34 · 860610.1021/bi00027a010 ↗
17. Sturtevant J. M. · Annu. Rev. Phys. Chem. · 1987 · 38 · 46310.1146/annurev.pc.38.100187.002335 ↗
18. Privalov P. L. · J. Adv. Protein Chem. · 1988 · 39 · 194
19. Yan G. · San Diego · 1995 · 602 · 256
20. Zoungrana T. · J. Colloid Interface Sci. · 1997 · 190 · 43710.1006/jcis.1997.4895 ↗
21. Steadman B. L. · Biotechnol. Bioeng. · 1992 · 40 · 810.1002/bit.260400103 ↗
22. Kondo A. · J. Colloid Interface Sci. · 1991 · 143 · 21410.1016/0021-9797(91)90454-G ↗
23. Nozaki Y. · Methods Enzymol. · 1972 · 26 · 4310.1016/S0076-6879(72)26005-0 ↗
24. Freskgård P.-O. · Biochemistry · 1994 · 33 · 1428110.1021/bi00251a041 ↗
25. Ptitsyn O. B. · Adv. Protein Chem. · 1995 · 47 · 8310.1016/S0065-3233(08)60546-X ↗
26. Kraulis P. J. · J. Appl. Chrystallogr. · 1991 · 24 · 1192