BioNMR

BioNMR (http://www.bionmr.com/forum/)
-   Journal club (http://www.bionmr.com/forum/journal-club-9/)
-   -   [NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment (http://www.bionmr.com/forum/journal-club-9/solid-state-nmr-studies-secondary-structure-mutant-prion-protein-fragment-9650/)

nmrlearner 11-19-2010 08:44 PM

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
 
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.

Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.

Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90

Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE

The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in randomly aggregated (dried from water) and fibrillar (precipitated from water/acetonitrile) forms by (13)C solid-state NMR. Recent studies have shown that the fibrillar form of the P101L mutant of MoPrP(89-143) is capable of inducing prion disease in transgenic mice, whereas unaggregated or randomly aggregated samples do not provoke disease. Through analysis of (13)C chemical shifts, we have determined that both wild-type and mutant sequence MoPrP(89-143) form a mixture of beta-sheet and alpha-helical conformations in the randomly aggregated state although the beta-sheet content in MoPrP(89-143, P101L) is significantly higher than in the wild-type peptide. In a fibrillar state, MoPrP(89-143, P101L) is completely converted into beta-sheet, suggesting that the formation of a specific beta-sheet structure may be required for the peptide to induce disease. Studies of an analogous peptide from Syrian hamster PrP verify that sequence alterations in residues 101-117 affect the conformation of aggregated forms of the peptides.

PMID: 11562491 [PubMed - indexed for MEDLINE]



Source: PubMed


All times are GMT. The time now is 11:31 PM.

Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013