Rapid folding of the prion protein captured by pressure-jump
Jenkins, David C., Pearson, David S., Harvey, Andrew, Sylvester, Ian D., Geeves, Michael A. and Pinheiro, Teresa J. T.. (2009) Rapid folding of the prion protein captured by pressure-jump. European Biophysics Journal, Vol.38 (No.5). pp. 625-635. ISSN 0175-7571Full text not available from this repository.
Official URL: http://dx.doi.org/10.1007/s00249-009-0420-6
The conversion of the cellular form of the prion protein (PrPC) to an altered disease state, generally denoted as scrapie isoform (PrPSc), appears to be a crucial molecular event in prion diseases. The details of this conformational transition are not fully understood, but it is perceived that they are associated with misfolding of PrP or its incapacity to maintain the native fold during its cell cycle. Here we present a tryptophan mutant of PrP (F198W), which has enhanced fluorescence sensitivity to unfolding/refolding transitions. Equilibrium folding was studied by circular dichroism and fluorescence. Pressure-jump experiments were successfully applied to reveal rapid submillisecond folding events of PrP at temperatures not accessed before.
|Item Type:||Journal Article|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)|
|Journal or Publication Title:||European Biophysics Journal|
|Number of Pages:||11|
|Page Range:||pp. 625-635|
|Access rights to Published version:||Restricted or Subscription Access|
|Funder:||Royal Society (Great Britain), Wellcome Trust, Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Engineering and Physical Sciences Research Council (EPSRC)|
|Grant number:||SHoWCAse 053914/Z/98/Z, 07021, 88/BS516471|
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