Friebel, Anne, Thomas Specht, Erik von Harbou, Kerstin Münnemann, and Hans Hasse. “Prediction of Flow Effects in Quantitative NMR Measurements.” Journal of Magnetic Resonance 312 (March 2020): 106683.
A method for the prediction of the magnetization in flow NMR experiments is presented, which can be applied to mixtures. It enables a quantitative evaluation of NMR spectra of flowing liquid samples even in cases in which the magnetization is limited by the flow. A transport model of the nuclei’s magnetization, which is based on the Bloch-equations, is introduced into a computational fluid dynamics (CFD) code. This code predicts the velocity field and relative magnetization of different nuclei for any chosen flow cell geometry, fluid and flow rate. The prediction of relative magnetization is used to correct the observed reduction of signal intensity caused by incomplete premagnetization in fast flowing liquids. By means of the model, quantitative NMR measurements at high flow rates are possible. The method is predictive and enables calculating correction factors for any flow cell design and operating condition based on simple static T1 time measurements. This makes time-consuming calibration measurements for assessing the influence of flow effects obsolete, which otherwise would have to be carried out for each studied condition. The new method is especially interesting for flow measurements with compact medium field NMR spectrometers, which have small premagnetization volumes. In the present work, experiments with three different flow cells in a medium field NMR spectrometer were carried out. Acetonitrile, water, and mixtures of these components were used as model fluids. The experimental results for the magnetization were compared to the predictions from the CFD model and good agreement was observed.
A highly versatile automatized setup for quantitative measurements of PHIP enhancements #SABRE #NMR
From The DNP-NMR Blog:
A highly versatile automatized setup for quantitative measurements of PHIP enhancements #SABRE #NMR
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Kiryutin, A.S., et al., A highly versatile automatized setup for quantitative measurements of PHIP enhancements. J. Magn. Reson., 2017. 285: p. 26-36.
https://www.ncbi.nlm.nih.gov/pubmed/29073504
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02-02-2018 11:31 PM
[NMR paper] Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy.
Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy.
Related Articles Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy.
J Phys Chem Lett. 2017 Nov 17;:
Authors: Mukhopadhyay D, Nadaud PS, Shannon MD, Jaroniec CP
Abstract
We demonstrate rapid quantitative measurements of site-resolved paramagnetic relaxation enhancements (PREs), which are a...
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11-19-2017 05:41 AM
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Abstract
Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ?/? torsion angles seen in intrinsically disordered proteins (IDPs). The ?/? torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and 3JHN-H? coupling constants for a...
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10-25-2017 10:14 PM
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins
Abstract
Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ?/? torsion angles seen in intrinsically disordered proteins (IDPs). The ?/? torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and 3JHN-H? coupling constants for a...
Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization
From The DNP-NMR Blog:
Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization
Miclet E, Abergel D, Bornet A, Milani J, Jannin S, Bodenhausen G. Toward Quantitative Measurements of Enzyme Kinetics by Dissolution Dynamic Nuclear Polarization. The Journal of Physical Chemistry Letters. 2014;5(19):3290-5.
http://dx.doi.org/10.1021/jz501411d
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06-03-2015 11:04 PM
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
Prediction of flow effects in quantitative NMR measurements #DNPNMR
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