Category Archives: solid-state DNP

Postdoctoral Position Available at the National High Magnetic Field Laboratory (NHMFL) on Magic-Angle Spinning Dynamic Nuclear Polarization (MAS-DNP)

From the Ampere Magnetic Resonance List

Postdoctoral Position Available at the National High Magnetic Field Laboratory (NHMFL) on Magic-Angle Spinning Dynamic Nuclear Polarization (MAS-DNP)

A postdoctoral position is available immediately at the NHMFL in Tallahassee Florida working on magic-angle spinning DNP. The NHMFL just received a 600MHz MAS DNP system. The candidate will develop applications utilizing the state-of-art equipment for bio-solids, materials/surface and small molecules and collaborate with users of NHMFL facilities and the DNP system. The candidate will join other scientists and engineers in a lab-wide initiative which also includes dissolution DNP and solution Overhauser DNP. Minority and female candidates are encouraged to apply. Please send applications to Zhehong Gan at gan@magnet.fsu.edu.

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Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces

Cheng, C.-Y., et al., Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces. Proc. Nat. Aca. Sci. USA, 2013. 110(42): p. 16838-16843.

http://www.pnas.org/content/110/42/16838.abstract

Knowing the topology and location of protein segments at water–membrane interfaces is critical for rationalizing their functions, but their characterization is challenging under physiological conditions. Here, we debut a unique spectroscopic approach by using the hydration dynamics gradient found across the phospholipid bilayer as an intrinsic ruler for determining the topology, immersion depth, and orientation of protein segments in lipid membranes, particularly at water–membrane interfaces. This is achieved through the site-specific quantification of translational diffusion of hydration water using an emerging tool, 1H Overhauser dynamic nuclear polarization (ODNP)-enhanced NMR relaxometry. ODNP confirms that the membrane-bound region of α-synuclein (αS), an amyloid protein known to insert an amphipathic α-helix into negatively charged phospholipid membranes, forms an extended α-helix parallel to the membrane surface. We extend the current knowledge by showing that residues 90–96 of bound αS, which is a transition segment that links the α-helix and the C terminus, adopt a larger loop than an idealized α-helix. The unstructured C terminus gradually threads through the surface hydration layers of lipid membranes, with the beginning portion residing within 5–15 Å above the phosphate level, and only the very end of C terminus surveying bulk water. Remarkably, the intrinsic hydration dynamics gradient along the bilayer normal extends to 20–30 Å above the phosphate level, as demonstrated with a peripheral membrane protein, annexin B12. ODNP offers the opportunity to reveal previously unresolvable structure and location of protein segments well above the lipid phosphate, whose structure and dynamics critically contribute to the understanding of functional versatility of membrane proteins.

Sensitivity enhancement in solution NMR: emerging ideas and new frontiers

Lee, J.H., Y. Okuno, and S. Cavagnero, Sensitivity enhancement in solution NMR: emerging ideas and new frontiers. J Magn Reson, 2014. 241(0): p. 18-31.

http://www.ncbi.nlm.nih.gov/pubmed/24656077

Modern NMR spectroscopy has reached an unprecedented level of sophistication in the determination of biomolecular structure and dynamics at atomic resolution in liquids. However, the sensitivity of this technique is still too low to solve a variety of cutting-edge biological problems in solution, especially those that involve viscous samples, very large biomolecules or aggregation-prone systems that need to be kept at low concentration. Despite the challenges, a variety of efforts have been carried out over the years to increase sensitivity of NMR spectroscopy in liquids. This review discusses basic concepts, recent developments and future opportunities in this exciting area of research.

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