lowering the temperature of the sample under the coalescence temperature (depends on the molecule) will give you more data, for example resolving temperature dependend J like N-H protons on amides.
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Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Abstract X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down...
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08-13-2011 02:47 AM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
J Biomol NMR. 2011 Aug 9;
Authors: Linden AH, Franks WT, Akbey U, Lange S, van Rossum BJ, Oschkinat H
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100*K. Protein dynamics are poorly understood...
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08-10-2011 12:30 PM
Slight mistuning of a cryogenic probe significantly perturbs the water 1H precession frequency
Slight mistuning of a cryogenic probe significantly perturbs the water 1H precession frequency
Abstract A shift of the water proton precession frequency is described that can introduce errors in chemical shifts derived using the water signal as the chemical shift reference. This shift, fs, arises as a consequence of radiation damping when the water proton and detector circuit resonance frequencies differ. Herein it is shown that experimental values of fs, measured as a function of detector circuit tuning offset for 500 and 900 MHz cryogenic probes, are in good agreement with theory. Of...
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01-09-2011 12:46 PM
[NMR paper] Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
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J Am Chem Soc. 2004 Jun 9;126(22):7119-25
Authors: Serber Z, Straub W, Corsini L, Nomura AM, Shimba N, Craik CS, Ortiz de Montellano P, Dötsch V
Studying protein components of large intracellular complexes by in-cell NMR has so far been impossible because the backbone resonances are unobservable due to their slow tumbling rates. We describe a methodology that overcomes...
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11-24-2010 09:51 PM
[Question from NMRWiki Q&A forum] Please suggest experiments that push the power limits of NMR probes
Please suggest experiments that push the power limits of NMR probes
I'm trying to come up with reasonable tests of probe performance for all channels by simulating conditions at which arcing is most likely to occur.
For those tests I usually read voltage of the incoming wave on the RF line using directional coupler with a 50dB attenuated pickup and oscilloscope after running an "experiment" pulsing at the power and duty cycle that simulates the condition to be tested. If the waveform looks nice and square - there is no arcing.
What experiments should I look into? OK for 1H I'd pick...
nmrlearner
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10-08-2010 02:35 AM
[NMR paper] Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfov
Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Use of paramagnetic NMR probes for structural analysis in cytochrome c3 from Desulfovibrio vulgaris.
Eur J Biochem. 1997 Mar 15;244(3):721-34
Authors: Salgueiro CA, Turner DL, Xavier AV
The dipolar field generated by each of the four haems in the tetrahaem ferricytochrome c3 from...
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08-22-2010 03:31 PM
[NMR paper] NMR identification of protein surfaces using paramagnetic probes.
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Biochemistry. 1990 Oct 30;29(43):10041-8
Authors: Petros AM, Mueller L, Kopple KD
Paramagnetic agents produce line broadening and thus cancellation of anti phase cross-peak components in two-dimensional correlated nuclear magnetic resonance spectra. The specificity of this effect was examined to determine its utility for identifying surface residues of proteins. Ubiquitin and hen egg white...
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08-21-2010 11:04 PM
Nitrogen-detected CAN and CON experiments as alternative experiments for main chain N
Abstract Heteronuclear direct-detection experiments, which utilize the slower relaxation properties of low γ nuclei, such as 13C have recently been proposed for sequence-specific assignment and structural analyses of large, unstructured, and/or paramagnetic proteins. Here we present two novel 15N direct-detection experiments. The CAN experiment sequentially connects amide 15N resonances using 13Cα chemical shift matching, and the CON experiment connects the preceding 13C� nuclei. When starting from the same carbon polarization, the intensities of nitrogen signals detected in the CAN or...
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