The amplitude of the 2H lock signal provides information for an electronic feedback circuit which continuously corrects the magnetic field strength (by way of a B0 shim) to compensate for environmental instability. A poor 2H lock signal will provide unreliable input for the feedback circuit and B0 compensation will be erratic. This leads to undesirable effects in NMR spectra. For example, noisy lock signals will lead to undesirable noise at the base of the observed NMR peaks. If one uses too much lock power, the 2H lock signal gets saturated and the lock amplitude is unstable. A saturated 2H lock will lead to problems in the NMR spectrum since the input to the B0 compensation feedback circuit is unstable. This is demonstrated in the figure below.
When one scan is collected, there are spectral distortions at the base of the NMR resonances. When 16 scans are collected these artifacts average to produce a general broadening at the base of the NMR resonances. Be careful not to saturate the 2H lock.
Chromophore Distortions in Photointermediates of Proteorhodopsin Visualized by Dynamic Nuclear Polarization-Enhanced Solid-State NMR #DNPNMR #NMR #SSNMR
From The DNP-NMR Blog:
Chromophore Distortions in Photointermediates of Proteorhodopsin Visualized by Dynamic Nuclear Polarization-Enhanced Solid-State NMR #DNPNMR #NMR #SSNMR
p.p1 {margin: 0.0px 0.0px 0.0px 36.0px; text-indent: -36.0px; font: 12.0px Helvetica}
Mehler, M., et al., Chromophore Distortions in Photointermediates of Proteorhodopsin Visualized by Dynamic Nuclear Polarization-Enhanced Solid-State NMR. J. Am. Chem. Soc., 2017. 139(45): p. 16143-16153.
https://www.ncbi.nlm.nih.gov/pubmed/29027800
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01-23-2018 02:57 AM
[NMR paper] Chromophore Distortions in Photointermediates of Proteorhodopsin visualized by DNP-enhanced solid-state NMR.
Chromophore Distortions in Photointermediates of Proteorhodopsin visualized by DNP-enhanced solid-state NMR.
Chromophore Distortions in Photointermediates of Proteorhodopsin visualized by DNP-enhanced solid-state NMR.
J Am Chem Soc. 2017 Oct 13;:
Authors: Mehler M, Eckert CE, Leeder AJ, Kaur J, Fischer T, Kubatova N, Brown LJ, Brown RCD, Becker-Baldus J, Wachtveitl J, Glaubitz C
Abstract
Proteorhodopsin (PR) is the most abundant retinal protein on earth and functions as a light-driven proton pump. Despite of extensive efforts,...
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10-16-2017 01:27 AM
[Question from NMRWiki Q&A forum] Strange peak distortions but that of water
Strange peak distortions but that of water
Hy everyone, I'm having a strange problem when reading the NMR spectrum of a small aromatic molecule in deuterium oxide: all the resonances of the solute molecule are very distorted, as if caused by poor shimming. For example, they show multiple maxima, and are not symmetric. But the problem is that the HDO resonance has a perfectly symmetric Lorentzian lineshape. Could it be a shimming problem, even if the water resonance is perfect?
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07-05-2013 08:03 AM
[Question from NMRWiki Q&A forum] DOSY deep signal distortions
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Hi heveryone,I'm trying to run some DOSY experiments, but the resulting spectra are VERY distorted, and this is not just a problem of phase. The strange thing is that these distortions didn't appear as long as a few days ago... Have you got any suggestion?Further details: The spectrometer is a Bruker 400MHz, and the sequence is the dstegp3s
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06-26-2013 09:39 AM
[Question from NMRWiki Q&A forum] lose the lock
lose the lock
Recently the TOPSPIN always popup a windows "L-TRX board overtemperature error occurs"Then the lock is lost, and the locl level reduced from 90% to 10%.I couldn't figure out the problem.I am using the Bruker Advance III spectrometer.Thank you!
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12-31-2012 12:23 PM
[Question from NMRWiki Q&A forum] NMR Lock signal
NMR Lock signal
THis is my lock signal....what is up with it, and what do I do?https://picasaweb.google.com/113100759436397078363/LockSignal02#slideshow/5631842657786659330
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07-21-2011 10:31 PM
[Question from NMRWiki Q&A forum] NMR resonance Lock
NMR resonance Lock
I am running a varian gemini 300 on SUN microsystems with UNIX. I am trying to lock on my sample, and my lock is not showing up as a "step" as usual. Instead, it has troughs in it. What are some options in fixing this, or is this acceptable?
-Jon K.
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06-07-2011 01:01 AM
[NMR paper] Refinement of the NMR solution structure of a protein to remove distortions arising f
Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motion.
Related Articles Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motion.
Biochemistry. 1991 Apr 23;30(16):3807-11
Authors: Fejzo J, Krezel AM, Westler WM, Macura S, Markley JL
The effect of internal motion on the quality of a protein structure derived from nuclear magnetic resonance (NMR) cross relaxation has been investigated experimentally. Internal rotation of the...