From the Ampere Magnetic Resonance List
Postdoctoral position in biological MAS ssNMR
The Van der Wel lab is looking for potential postdoctoral researchers with a background and/or interest in advanced magic-angle-spinning solid-state NMR. As described below, there are two different NIH-funded research projects available, focused either on protein aggregation and amyloid formation, or on mitochondrial protein-lipid interactions. Applications are sought from individuals with expertise in biological solid-state NMR (preferred), or in biomolecular solution NMR. Highly qualified individuals with a strong track record in biophysical or biochemical studies of protein aggregation/membrane proteins may also be suitable.
Potentially interested parties are encouraged to contact me with (informal) inquiries by email at email@example.com. I will also be available to discuss things in person at either EUROMAR or the Rocky Mountain ssNMR conference.
Patrick van der Wel
Postdoctoral opportunities in biomolecular solid-state NMR
One or more postdoctoral position(s) are available in the Van der Wel solid-state NMR research group in the Department of Structural Biology of the University of Pittsburgh School of Medicine.
The researcher(s) will join the Van der Wel lab to contribute to our NIH-funded research projects. The first project is focused on the structural and mechanistic studies of amyloid formation and protein aggregation, with a particular focus on polyglutamine-expanded proteins implicated in Huntington’s Disease. The second project studies mitochondrial protein- lipid interactions critical to the early stages of apoptosis, with implications for neurodegenerative disease and cancer research. Common to both projects, and most of our research, is a central use of advanced magic-angle-spinning (MAS) solid-state NMR spectroscopy. Crucial biological insights regarding the structure and dynamics of aggregated and membrane-bound proteins are obtained via state-of-the-art ssNMR measurements of relaxation rates, dipolar order parameters, intra- and intermolecular distance constraints, and backbone and side-chain torsion angles.
Related recent publications:
Hoop et al. (2016) Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. PNAS 113(6); 1546.
Mandal et al. (2015) Structural changes and pro-apoptotic peroxidase activity of cardiolipin-bound mitochondrial cytochrome c. Biophys. J. 109(9): 1873.
Resources & Location:
The Van der Wel lab uses departmental wide-bore 600MHz and 750MHz Bruker ssNMR spectrometers outfitted with 3.2, 1.9, and 1.3 mm CP/MAS as well as static ssNMR probes. Departmental facilities offer state-of-the-art EM, X-ray and solution NMR instrumentation, with the latter including 700, 800, and 900 MHz spectrometers. Excellent resources are available for protein production, biophysical and computational studies. The lab is housed in the interdisciplinary Dept of Structural Biology, one of the basic science departments of the University of Pittsburgh School of Medicine. The department and the school of medicine are located in walking distance of the main campuses of both the University of Pittsburgh and Carnegie Mellon University, providing a fertile collaborative research environment.
A strong preference is given to candidates with experience with biomolecular multidimensional ssNMR techniques. A strong interest or experience in the areas of disease-associated protein aggregation and/or membrane-protein structure and function is a bonus. Highly qualified candidates who have a background in solution-state NMR or other structural biology methods, and have in interest in the above topics, are also encouraged to apply.
For more detailed information on these projects, links to related publications, and other useful information please visit the lab website at http://www.vanderwellab.org. To apply, or to obtain more information, please contact Patrick van der Wel by email at firstname.lastname@example.org. Applications are expected to include a cover letter (or “cover email”) explaining specific research interests, a CV, and the names and contact information for three reference writers.
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