Hi, I have question for you who have Bruker instruments! On 300 MHz I worked on selective noesy pulse sequence (selnogp) and it worked perfectly (d20=0.05s, pl14=62dB and p12=90ms).When I tried it to do on 600 MHz, it did not work. Please, help me to understand it! Marijana
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[Question from NMRWiki Q&A forum] 1D NOESY with selective excitation and water suppression
1D NOESY with selective excitation and water suppression
Hi,
I am trying to collect 1D NOESY spectrum of a small protein in 90% H2O with selective excitation so I could follow a few NOEs without running a whole 2D experiment. Is there any sequence in Varian BioPack that I could use for that? I cannot achieve water suppression with the standard 'Noesy1D' sequence and all the other seem to not allow to selectively irradiate only one peak. Maybe it is just a matter of right parameters but I don't know how to set them properly - if so I will appreciate any advice.
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[U. of Ottawa NMR Facility Blog] 19f noesy
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Two-dimensional 1H NOESY data are routinely used to assign specific stereo-isomers based on the proton nuclear Overhauser effects (NOE's) which are strongly correlated to inter-proton distances through space. For example, NOE's may be observed for cis- protons across a double bond but not observed for trans- protons. The same technique can be used with 19F in fluorinated compounds to gauge the inter-fluorine distance and assign stereochemistry. The figure below shows the 19F NOESY spectrum of a fluorine containing cobalt complex.
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[Question from NMRWiki Q&A forum] N15 NNH separated NOESY
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I came across one reference which describe N15 NNH separated NOESY experiment but I am not able to get more information about this experiment from other sources. Is this experiment useful for providing restraints for protein structure calculation. what kind of information this experiment can provide and how to set up. If anyone has references to suggest, please suggest.
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[Question from NMRWiki Q&A forum] Auto peak picking of N15Edit NOESY and C13 Edit NOESY spectrum
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[Question from NMRWiki Q&A forum] NOESY+WET 2D artifacts
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Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
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Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
J Magn Reson. 2011 Mar 17;
Authors: Traaseth NJ, Veglia G
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Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 March 2011</br>
Nathaniel J., Traaseth , Gianluigi, Veglia</br>
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR spectra of membrane proteins in fluid lipid membranes with broad lines and...