Dynamics of oligomer formation by denatured carbonic anhydrase II

Aggregation and subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. Many proteins unrelated to amyloidoses also fibrillate at the appropriate conditions. These proteins serve as a model for studying the processes of pro...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2008-05, Vol.1784 (5), p.834-842
Main Authors: Prokhorov, Dmitry A., Timchenko, Alexander A., Uversky, Vladimir N., Khristoforov, Vladimir S., Kihara, Hiroshi, Kimura, Kazumoto, Kutyshenko, Viktor P.
Format: Article
Language:English
Subjects:
Amyloid-like structure
Animals
Carbonic anhydrase II
Carbonic Anhydrase II - chemistry
Carbonic Anhydrase II - metabolism
Cattle
Circular Dichroism
Magnetic Resonance Spectroscopy
NMR
Protein association
Protein Denaturation - drug effects
Protein Folding
Protein Structure, Quaternary
Scattering, Small Angle
Small angle X-ray scattering
Spin diffusion
Time Factors
Urea - pharmacology
X-Ray Diffraction
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Summary:Aggregation and subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. Many proteins unrelated to amyloidoses also fibrillate at the appropriate conditions. These proteins serve as a model for studying the processes of protein misfolding, oligomerization and fibril formation. The accumulated data support the model where protein fibrillogenesis proceeds via the formation of a relatively unfolded amyloidogenic conformation. The urea-induced unfolding of bovine carbonic anhydrase II, BCA II, is characterized by a combination of high-resolution NMR, circular dichroism spectroscopy and small angle X-ray scattering. It is shown that the formation of associates of protein molecules in complex with solvent (water and urea), APS, takes place in the presence of 4–6 M urea. The subsequent increase in urea concentration to 8 M is accompanied by a disruption of APS and leads to a complete unfolding of a protein molecule. Analysis of BCA II self-association in the presence of 4.2 M urea revealed that APS are relatively large mostly β-structural blocks with the averaged molecular mass of 190–220 kDa. This work also demonstrates some novel NMR-based methodological approaches that provide useful information on protein self-association.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/j.bbapap.2008.02.012