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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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Prof. Christopher Jaroniec, The Ohio State University
Atomic-resolution studies of protein structure and dynamics by magic-angle spinning solid-state NMR spectroscop
Physical Chemistry Seminar Series
Solid-state nuclear magnetic resonance (SSNMR) has recently emerged as a unique spectroscopic tool, with great potential for providing atomic-resolution images of biomacromolecules that are not amenable to characterization by traditional high-resolution methods. I will discuss the basics of biomolecular magic-angle spinning SSNMR spectroscopy and describe our recent studies aimed at the detailed characterization of amyloid aggregates formed by the Y145Stop mutant of prion protein (PrP).1 This particular PrP variant is associated with the development of a heritable cerebral amyloidosis in humans, and, importantly, has been shown to provide an experimentally-tractable in vitro model for investigating the phenomena of prion strains and transmissibility barriers in mammalian prion propagation. I will also discuss our recent SSNMR studies of natively diamagnetic proteins intentionally modified with covalently-bound paramagnetic tags, including nitroxide spin labels and transition metal ions.2 The primary aim of these studies is to develop new SSNMR methodologies that exploit the nuclear paramagnetic relaxation enhancement (PRE) phenomenon to obtain long-range (up to ~20 Ã ) structural restraints inaccessible by conventional SSNMR methods, and to utilize these PRE restraints for SSNMR protein structure refinement.
1)Helmus et al. Proc. Natl. Acad. Sci. USA 2008, 105, 6284-6289; Helmus et al. J. Am. Chem. Soc. 2010, 132, 2393-2403.
2)Nadaud et al. J. Am. Chem. Soc. 2007, 129, 7502-7503; Nadaud et al. J. Am. Chem. Soc. 2009, 131, 8108-8120; Nadaud et al. J. Am. Chem. Soc. 2010, 132, 9561-9563.
For more information contact Prof. Rigoberto Hernandez (404-894-0594) or Prof. Angelo Bongiorno (404-385-5169).
