Eichhorn, T.R., et al., An apparatus for pulsed ESR and DNP experiments using optically excited triplet states down to liquid helium temperatures. J. Magn. Reson., 2013. 234(0): p. 58-66.
In standard Dynamic Nuclear Polarization (DNP) electron spins are polarized at low temperatures in a strong magnetic field and this polarization is transferred to the nuclear spins by means of a microwave field. To obtain high nuclear polarizations cryogenic equipment reaching temperatures of 1 K or below and superconducting magnets delivering several Tesla are required. This equipment strongly limits applications in nuclear and particle physics where beams of particles interact with the polarized nuclei, as well as in neutron scattering science. The problem can be solved using short-lived optically excited triplet states delivering the electron spin. The spin is polarized in the optical excitation process and both the cryogenic equipment and magnet can be simplified significantly. A versatile apparatus is described that allows to perform pulsed dynamic nuclear polarization experiments at X-band using short-lived optically excited triplet sates. The efficient 4He flow cryostat that cools the sample to temperatures between 4 K and 300 K has an optical access with a coupling stage for a fiber transporting the light from a dedicated laser system. It is further designed to be operated on a neutron beam. A combined pulse ESR/DNP spectrometer has been developed to observe and characterize the triplet states and to perform pulse DNP experiments. The ESR probe is based on a dielectric ring resonator of 7 mm inner diameter that can accommodate cubic samples of 5 mm length needed for neutron experiments. NMR measurements can be performed during DNP with a coil integrated in the cavity. With the presented apparatus a proton polarization of 0.5 has been achieved at 0.3 T.
Liquid State DNP for Water Accessibility Measurements on Spin-labeled Membrane Proteins at Physiological Temperatures
Liquid State DNP for Water Accessibility Measurements on Spin-labeled Membrane Proteins at Physiological Temperatures
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Andrin Doll, Enrica Bordignon, Benesh Joseph, René Tschaggelar, Gunnar Jeschke</br>
We demonstrate the application of continuous wave dynamic nuclear polarization (DNP) at 0.35 Tesla for site-specific water accessibility studies on spin-labeled membrane proteins at concentrations in the 10-100 micromolar range. The DNP effects at such low concentrations are weak and the experimentally...
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06-16-2012 06:01 AM
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1Ï?: an application to αB-crystallin
Abstract Carr-Purcell-Meiboom-Gill relaxation dispersion (CPMG RD) NMR spectroscopy has emerged as a powerful tool for quantifying the kinetics and thermodynamics of millisecond time-scale exchange processes involving the interconversion between a visible ground state and one or more minor, sparsely populated invisible â??excitedâ?? conformational states. Recently it has also become possible to determine atomic resolution...
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04-09-2012 01:19 AM
Magneto-optical contrast in liquid-state optically detected NMR spectroscopy [Applied Physical Sciences]
Magneto-optical contrast in liquid-state optically detected NMR spectroscopy
Pagliero, D., Meriles, C. A....
Date: 2011-12-06
We use optical Faraday rotation (OFR) to probe nuclear spins in real time at high-magnetic field in a range of diamagnetic sample fluids. Comparison of OFR-detected NMR spectra reveals a correlation between the relative signal amplitude and the fluid Verdet constant, which we interpret as a manifestation of the variable detuning between the probe beam and the sample optical transitions. The analysis of chemical-shift-resolved, optically detected spectra allows...
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12-06-2011 08:04 PM
[U. of Ottawa NMR Facility Blog] Resolution During a Liquid Helium Refill
Resolution During a Liquid Helium Refill
Students sometimes ask whether or not they can collect NMR data during a liquid helium refill. The answer depends on the type of NMR experiment. For most solids experiments, where high resolution (
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09-14-2011 09:34 PM
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.
Biochim Biophys Acta. 2011 Aug 3;
Authors: Gustavsson M, Traaseth NJ, Veglia G
In this paper, we analyzed the ground and excited states of phospholamban (PLN), a membrane protein that regulates sarcoplasmic reticulum calcium ATPase (SERCA), in different membrane mimetic environments....
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08-16-2011 01:19 PM
[NMR paper] Studying excited states of proteins by NMR spectroscopy.
Studying excited states of proteins by NMR spectroscopy.
Related Articles Studying excited states of proteins by NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):932-5
Authors: Mulder FA, Mittermaier A, Hon B, Dahlquist FW, Kay LE
Protein structure is inherently dynamic, with function often predicated on excursions from low to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 lysozyme, L99A, show that the cavity is sterically inaccessible to ligand, yet the protein is able to bind substituted benzenes rapidly....
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11-19-2010 08:44 PM
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Patrik Lundström, D. Flemming Hansen and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 42(1); pp 35 - 47
Abstract: Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy has emerged as a powerful method for quantifying chemical shifts of excited protein states. For many applications of the technique that involve the measurement of relaxation rates of carbon...
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09-21-2008 11:36 PM
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
D. Flemming Hansen, Pramodh Vallurupalli and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 41(3); pp 113 - 120
Abstract:
Currently the main focus of structural biology is the determination of static three-dimensional representations of biomolecules that for the most part correspond to low energy (ground state) conformations. However, it is becoming increasingly well recognized that higher energy structures often play important roles in function as well. Because these conformers...