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My research focuses on the development of solid-state NMR methodology and its applications to studying relationships between structure, dynamics and activity of biomolecular systems. I am particularly interested in atomic resolution characterization of solid and solid-liquid interface biological systems including, but not limited to, amyloid fibrils and membrane proteins. Membrane proteins perform crucial functions such as signaling and transport of materials across membrane. Amyloid fibrils, a primer in self-assembling systems, are probably best known for their implication in debilitating neurodegenerative diseases such as Alzheimer’s or Parkinson’s. However, they are also involved in normal physiological processes such as biosynthesis of melanin. Understandably, both membrane proteins and amyloid fibrils captivate not only for their intriguing biophysics, but also for their medical relevance, e.g. over 50% of all drug targets act on membrane–bound receptors. However, they often lack long-range crystallinity and are insoluble and therefore, not easily amenable to detailed structural characterization by the traditional biophysical methods such as single-crystal x-ray crystallography and solution NMR. At the same, often even in the absence of long-range order they exhibit sufficient local order to allow for detailed atomic resolution description of both structure and dynamics by solid-state NMR.
Ph.D. positions available.
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Site-specific Measurement of Slow Motions in Proteins. Lewandowski JR, Sass HJ, Grzesiek S, Blackledge M, Emsley J. Am. Chem. Soc. 2011 133:16762-16765. doi://10.1021/ja206815h
Structural Complexity of a Composite Amyloid Fibril Lewandowski JR, van der Wel PC a, Rigney M, Grigorieff N, Griffin RG J. Am. Chem. Soc. 2011 133: 9457-9469. doi://10.1021/ja203736z
Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein Lewandowski JR, Sein J, Sass HJ, Grzesiek S, Blackledge M, Emsley L J. Am. Chem. Soc. 2010 132:8252-4. doi://10.1021/ja102744b
High-resolution solid-state NMR structure of a 17.6 kDa protein Bertini I, Bhaumik A, De Paëpe G, Griffin RG, Lelli M, Lewandowski JR, Luchinat C J. Am. Chem. Soc. 2010 132:1032-40. doi://10.1021/ja906426p
Proton assisted recoupling and protein structure determination De Paëpe G, Lewandowski JR, Loquet A, Böckmann A, Griffin RG J. Chem. Phys. 2008 129:245101. doi://10.1063/1.3036928
Proton assisted insensitive nuclei cross polarization Lewandowski JR, De Paëpe G, Griffin RG J. Am. Chem. Soc. 2007 129:728-9. doi://10.1021/ja0650394
Dynamic nuclear polarization of amyloidogenic peptide nanocrystals: GNNQQNY, a core segment of the yeast prion protein Sup35p van Der Wel PCA, Lewandowski JR, Hu K-N, Griffin RG J. Am. Chem. Soc. 2006 128:10840-6. doi://10.1021/ja0626685
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