New GHz-class NMR Capabilities Open New Research Frontiers in Structural Biology, Intrinsically Disordered Proteins (IDP) and Membrane Proteins
PITTSBURGH, PA – April 11, 2016 – At the 57th Experimental Nuclear Magnetic Resonance Conference (www.enc-conference.org), Bruker announced new GHz-class NMR magnet and probe technologies to enable expanding frontiers in structural biology, membrane protein and intrinsically disordered protein (IDP) research.
World's first shielded 1 GHz NMR at University of Bayreuth: Bruker has successfully installed the world’s first, next-generation 1GHz NMR system equipped with an actively-shielded Aeon™ 1 GHz magnet at the University of Bayreuth, Germany. Active shielding reduces the space requirements for the two-story magnet by more than an order of magnitude, and makes siting of next-generation Aeon 1 GHz magnets straightforward. The new Aeon 1 GHz magnets have been developed using advanced superconductors provided by Bruker’s Energy & Supercon Technologies (BEST) division. The Aeon 1 GHz also features novel active refrigeration technology, eliminating the need for liquid nitrogen, and reducing liquid helium boil-off essentially to zero under normal operation. Bi-annual pulse-tube cooler maintenance is done at field for minimal disruption and downtime.
New 15N-optimized CryoProbe™: The recently introduced next-generation 15N optimized CryoProbes with cold 15N preamplifiers will now be offered up to 1 GHz. In conjunction with the latest GHz-magnets and novel 15N direct-detect NMR methods, this CryoProbe now makes direct 15N detection sensitive and advantageous in very large globular proteins and in IDPs, due to the longer relaxation times, high resolution and low chemical shift anisotropy of 15N spectra. Furthermore, 15N detection is beneficial in cases where carbon-detected methods suffer from multiple couplings to neighboring carbons, or in the study of proline-rich protein domains. Another attractive area of 15N detection are paramagnetic metallo-proteins, where 1H or even 13C magnetization is broadened beyond detection limits. These 15N-detected experiments are critically dependent on the high sensitivity delivered by new 5mm CryoProbes with cryogenic 15N preamplifiers. In conjunction with updated fast acquisition methods, experiment times are no longer a detriment to arrive at this information.
Professor Gerhard Wagner of Harvard Medical School, a pioneer of 15N direct detection, stated: “Direct 15N and 13C detection methods have recently been evolved and found to be almost as sensitive as 1H detection techniques, benefitting from the slow transverse relaxation. 15N-detected TROSYs in particular do not require protein perdeuteration, which avoids the confounding problem of incomplete amide back exchange in large proteins that cannot be refolded and open avenues for expressing [13C,15N]-labeled proteins in insect cells or mammalian systems. The low-gamma NMR detection methods also provide new opportunities for studies of proline-rich polypeptides often found in regulatory regions, such as phosphorylation domains. However, spectra of such domains are typically poorly dispersed and highest field strengths will be needed to reveal mechanisms of phosphorylation-dependent switch mechanisms. Availability of GHz-class NMR instruments will be important for revealing mechanisms of phosphorylation-dependent signaling switches.”
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Professor Gerhard Wagner of Harvard Medical School, a pioneer of 15N direct detection, stated: “Direct 15N and 13C detection methods have recently been evolved and found to be almost as sensitive as 1H detection techniques, benefitting from the slow transverse relaxation. 15N-detected TROSYs in particular do not require protein perdeuteration, which avoids the confounding problem of incomplete amide back exchange in large proteins that cannot be refolded and open avenues for expressing [13C,15N]-labeled proteins in insect cells or mammalian systems. The low-gamma NMR detection methods also provide new opportunities for studies of proline-rich polypeptides often found in regulatory regions, such as phosphorylation domains. However, spectra of such domains are typically poorly dispersed and highest field strengths will be needed to reveal mechanisms of phosphorylation-dependent switch mechanisms. Availability of GHz-class NMR instruments will be important for revealing mechanisms of phosphorylation-dependent signaling switches.”
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