Jenkins, David C. and Pearson, D.S. and Harvey, Andrew and Sylvester, Ian D. and Geeves, M.A. and Pinheiro, Teresa J. T. (2009) Rapid folding of the prion protein captured by pressure-jump. European Biophysics Journal, 38 (5). pp. 625-635. ISSN 0175-7571.
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The conversion of the cellular form of the prion protein (PrP(C)) to an altered disease state, generally denoted as scrapie isoform (PrP(Sc)), 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.
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||26 Apr 2012 14:59|
|Last Modified:||02 May 2012 10:30|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/29364 (The current URI for this page, for reference purposes)|
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