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 0175-7571

Full text not available from this repository.

Abstract

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
Publisher:	Springer
ISSN:	0175-7571
Date:	June 2009
Volume:	Vol.38
Number:	No.5
Number of Pages:	11
Page Range:	pp. 625-635
Identification Number:	10.1007/s00249-009-0420-6
Status:	Peer Reviewed
Publication Status:	Published
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
URI:	http://wrap.warwick.ac.uk/id/eprint/28026

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item