Katsikis, S., et al., Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device. Appl. Magn. Reson., 2015. 46(7): p. 723-729.
Dissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical optimizations in order to use dissolution DNP for biochemical and chemical applications. Here we show how a newly designed pressure dissolution kit considerably improves spectral quality and stability by enabling highly reliable and fast sample transfer to the NMR system.
Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device
From The DNP-NMR Blog:
Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device
Katsikis, S., et al., Improved Stability and Spectral Quality in Ex Situ Dissolution DNP Using an Improved Transfer Device. Appl. Magn. Reson., 2015: p. 1-7.
http://dx.doi.org/10.1007/s00723-015-0680-5
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06-25-2015 05:28 AM
[NMR paper] Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.
Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.
Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.
J Biomol NMR. 2015 Apr 11;
Authors: Mareuil F, Malliavin TE, Nilges M, Bardiaux B
Abstract
In biological NMR, assignment of NOE cross-peaks and calculation of atomic conformations are critical steps in the determination of reliable high-resolution structures. ARIA is an automated approach that performs NOE assignment and structure calculation in...
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04-12-2015 04:41 PM
Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA
Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA
Abstract
In biological NMR, assignment of NOE cross-peaks and calculation of atomic conformations are critical steps in the determination of reliable high-resolution structures. ARIA is an automated approach that performs NOE assignment and structure calculation in a concomitant manner in an iterative procedure. The log-harmonic shape for distance restraint potential and the Bayesian weighting of distance restraints, recently introduced in ARIA, were shown to...
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04-11-2015 12:04 AM
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways
HNCA+, HNCO+, and HNCACB+ experiments: improved performance by simultaneous detection of orthogonal coherence transfer pathways
Abstract
Three experiments, BESTâ??TROSY HNCA+, HNCO+ and HNCACB+ are presented for sequential backbone resonance assignment of 13C, 15N labelled proteins. The novelty of these experiments with respect to conventional pulse sequences is the detection of additional orthogonal coherence transfer pathways that results in enhanced sensitivity for sequential correlations without significantly compromising the intensity of...
An improved algorithm for MFR fragment assembly
An improved algorithm for MFR fragment assembly
Abstract A method for generating protein backbone models from backbone only NMR data is presented, which is based on molecular fragment replacement (MFR). In a first step, the PDB database is mined for homologous peptide fragments using experimental backbone-only data i.e. backbone chemical shifts (CS) and residual dipolar couplings (RDC). Second, this fragment library is refined against the experimental restraints. Finally, the fragments are assembled into a protein backbone fold using a rigid body docking algorithm using the RDCs as...
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05-17-2012 08:40 AM
[CNS Yahoo group] Improved EM-related resources at PDBe
Improved EM-related resources at PDBe
Hi all, The Protein Data Bank in Europe (PDBe; http://pdbe.org) continues to improve its services to the scientific community. As part of our recent website
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08-11-2011 02:24 AM
[NMR paper] 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenin
31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Related Articles 31P NMR saturation-transfer study of the in situ kinetics of the mitochondrial adenine nucleotide translocase.
Biochemistry. 1991 Aug 27;30(34):8351-7
Authors: Masiakos PT, Williams GD, Berkich DA, Smith MB, LaNoue KF
The exchange of intramitochondrial ATP (ATP(in)) for extramitochondrial ATP (ATP(out)) was measured by using 31P NMR spectroscopy over a range of temperatures in isolated rat liver mitochondria oxidizing...