Rienstra, Chad

Department of Chemistry
Ph.D. (1999), MIT (Chemistry)

   Research Topics

   Research Interests  

   The Rienstra group develops novel solid-state nuclear magnetic resonance (SSNMR) methods to solve previously intractable problems in biomolecular structure. Our high field, magic-angle spinning experiments resolve hundreds to thousands of sites in proteins that are not suitable for other high-resolution techniques, such as solution NMR and X-ray crystallography. Our highly interdisciplinary program draws together technologies from engineering, physics, chemistry, computer science and biology, yielding unique capabilities to address the following applications: (1) Nanocrystalline protein structure and dynamics. We have reported the highest resolution spectra of a solid protein thus far, and are proceeding to determine its structure at a resolution unattainable by any other method. Tensorial properties—including chemical shift anisotropies and dipolar couplings—are being measured at hundreds of sites simultaneously, to lend insight into structure and dynamics with unprecedented fidelity. (2) Fibrous (misfolded) proteins. We are investigating proteins associated with neurodegeneration, including a -synuclein, to characterize the structural and dynamic features distinguishing its wild-type form from the mutants that are known to cause early-onset Parkinson’s disease (PD). Synuclein is examined in physiologically relevant, membrane-associated and fibrillar forms. (3) Membrane proteins. Our new NMR probes enable, for the first time, high-field studies of membrane proteins in natural lipid environments. In many membrane proteins that are difficult or impossible to crystallize, we have acquired instrument-limited resolution. Examples include the 1,290-residue cytochrome bo 3 ubiquinol oxidase and membrane scaffolding proteins. We are pursuing complete structural studies, as well as targeted functional studies, in these systems. More information is available at http://www.scs.uiuc.edu/chem/rienstra.htm

  Key Words   NMR, protein structurem, dynamics, magic-angle spinning, membrane proteins

Current Funding: NSF, Eli Lilly,Research Corporation (Research Innovaiton and Cottrell Scholar Awards), American Chemical Society (Petroleum Research Fund), American Parkinson's Disease Association, National Parkinson Foundation, Branfman Foundation (for PD research), National Center for Supercomputing Applications

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