Fast and accurate algorithm for the simulation of NMR spectra of large spin systems.
J Magn Reson. 2011 Apr;209(2):123-30
Authors: Castillo AM, Patiny L, Wist J
The computational cost for the simulation of NMR spectra grows exponentially with the number of nuclei. Today, the memory available to store the Hamiltonian limits the size of the system that can be studied. Modern computers enable to tackle systems containing up to 13 spins [1], which obviously does not allow to study most molecules of interest in research. This issue can be addressed by identifying groups of spins or fragments that are not or only weakly interacting together, i.e., that only share weakly coupled spin pairs. Such a fragmentation is only permitted in the weak coupling regime, i.e., when the coupling interaction is weak compared to the difference in chemical shift of the coupled spins. Here, we propose a procedure that removes weak coupling interactions in order to split the spin system efficiently and to correct a posteriori for the effect of the neglected couplings. This approach yields accurate spectra when the adequate interactions are removed, i.e., between spins only involved in weak coupling interactions, but fails otherwise. As a result, the computational time for the simulation of 1D spectra grows linearly with the size of the spin system.
Suppression of sampling artefacts in high-resolution four-dimensional NMR spectra using Signal Separation Algorithm
Suppression of sampling artefacts in high-resolution four-dimensional NMR spectra using Signal Separation Algorithm
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 20 October 2011</br>
Jan*Stanek, Rafal*Augustyniak, Wiktor*Ko?mi?ski</br>
The development of non-uniform sampling (NUS) strategies permits to obtain high-dimensional spectra with increased resolution in significantly reduced experimental time. We extended a previously proposed signal separation algorithm (SSA) to process sparse four-dimensional NMR data. It is employed for two experiments...
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10-22-2011 10:16 AM
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
Multi-dimensional NMR without coherence transfer: Minimizing losses in large systems.
J Magn Reson. 2011 Jul 21;
Authors: Liu Y, Prestegard JH
Most multi-dimensional solution NMR experiments connect one dimension to another using coherence transfer steps that involve evolution under scalar couplings. While experiments of this type have been a boon to biomolecular NMR the need to work on ever larger systems pushes the limits of these procedures. Spin relaxation...
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08-13-2011 12:57 PM
Continuous-wave EPR at 275 GHz: Application to high-spin Fe3+ systems
Continuous-wave EPR at 275 GHz: Application to high-spin Fe3+ systems
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 11 March 2011</br>
G., Mathies , H., Blok , J.A.J.M., Disselhorst , P., Gast , H., van der Meer , ...</br>
The 275 GHz electron-paramagnetic-resonance spectrometer we reported on in 2004 has been equipped with a new probe head, which contains a cavity especially designed for operation in continuous-wave mode. The sensitivity and signal stability that is achieved with this new probe head is illustrated...
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03-12-2011 05:21 PM
[NMR paper] 1H,15N,13C-triple resonance NMR of very large systems at 900 MHz.
1H,15N,13C-triple resonance NMR of very large systems at 900 MHz.
Related Articles 1H,15N,13C-triple resonance NMR of very large systems at 900 MHz.
J Magn Reson. 2003 Aug;163(2):360-8
Authors: Chung J, Kroon G
We provide quantitative signal to noise data and feasibility study at 900 MHz for 1H-15N-13C triple resonance backbone assignment pulse sequences obtained from a medium sized 2H, 13C, 15N labeled protein slowed down in glycerol-water solution to mimic relaxation and spectroscopic properties of a much larger protein system with...
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11-24-2010 09:16 PM
[NMR paper] An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation
An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
Related Articles An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
J Am Chem Soc. 2002 Sep 11;124(36):10743-53
Authors: Korzhnev DM, Skrynnikov NR, Millet O, Torchia DA, Kay LE
Rotating-frame relaxation rates, R(1)(rho), are often measured in NMR studies of protein dynamics. We show here that large systematic errors can be introduced into measured values of heteronuclear R(1)(rho) rates using schemes which are...
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11-24-2010 08:58 PM
Sequential Assignment of Spin systems
hi,
I am new to the protein NMR Field.I want to assign spin numbers to 120 amonoacid residues of a protein.I am cluless how to assing these number to each.Could anyone help me? Here is the primary sequence f a protein domain-
ISLLAQRQQF WIQLEFHSRI TRGERHGVID HVGLGVQSQQ RSNGFLTSLC ILRPHYASLS LALEKAQLHS LLCEETDGEG TLEYGFMGQV KSRFTDLSRP NLFCRHLGQL LPLLRVCRDV
I am expecing your help.Thank you.
Fast and accurate algorithm for the simulation of NMR spectra of large spin systems.
Linear Mode
