کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801078 | 1054727 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The conversion of a monomeric α-helix-rich isoform to multimeric β-sheet-rich isoforms is a prominent feature of the conversion between PrPC and PrPSC. We mimicked this process in vitro by exposing an unglycosylated recombinant form of the full-length mouse prion protein (MoPrP23-231) to an acidic pH, at 37 °C, and we monitored the kinetics of conformational change and assembly. In these conditions, monomeric MoPrP23-231 converts slowly to two ensembles of soluble oligomers that are separated by size exclusion chromatography. The larger oligomers (I) are unstable, and their formation involves almost no change in secondary structure content. The smaller oligomers (II) form stable spherical or annular particles containing between 8 and 15 monomers as determined by multi-angle laser light scattering (MALLS). Their formation is concomitant with the main, thought limited, change in the secondary structure content (10%) seen by Fourier Transform Infrared (FTIR) spectroscopy. Even if these oligomers conserve a large part of the secondary structure of monomeric PrP, they exhibit amyloid features with the appearance of intermolecular β-structure as revealed by the appearance of an IR band below 1620 cmâ1.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1724, Issue 3, 5 August 2005, Pages 355-366
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1724, Issue 3, 5 August 2005, Pages 355-366
نویسندگان
Charlotte Vendrely, Hélène Valadié, Lucie Bednarova, Laurent Cardin, Marielle Pasdeloup, Jéremy Cappadoro, Jan Bednar, Marguerite Rinaudo, Marc Jamin,