Abstract:
:Using circular dichroism, fluorescence, and infrared spectroscopies, we studied the secondary structure of purified hamster PrP(C) in the presence of the mild, nonionic detergent octylglucoside. Under these native conditions, PrP(C) displayed an unexpectedly high beta-sheet component, intermediate between the values previously reported for PrP(Sc) and an isoform of PrP(C) isolated in a zwitterionic detergent. The structure of PrP(C) appeared to depend strongly on the detergent and/or phase. Switching from octylglucoside to zwitterion 3-14 drastically modified PrP secondary structure by increasing the alpha-helix while abolishing the beta-sheet component. In contrast, the conformation of PrP(C) in zwitterion was highly stable, since reverting to octylglucoside did not restore the original native structure. These and other results show that native PrP(C) in octylglucoside has some of the conformational characteristics that make the protein susceptible to conversion into PrP(Sc). Most importantly, this is the first study to demonstrate the intrinsic plasticity of the full-length native PrP(C) isolated from animal brains.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Pergami P,Bramanti E,Ascoli GAdoi
10.1006/bbrc.1999.1430subject
Has Abstractpub_date
1999-11-02 00:00:00pages
972-8issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(99)91430-4journal_volume
264pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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