Related Articles1H,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 macromolecular tumbling correlation time of 52 and 80 ns, respectively, at 296 and 283 K (corresponding to molecular weights of 130 and 250 kDa). Comparisons of several different schemes for transferring magnetization from proton to nitrogen and back to proton confirms Yang and Kay's 1999 prediction that avoiding the unfavorable relaxation properties of 1H-15N multiple quantum coherence in the TROSY phase cycle of the final 15N-1H transfer before acquisition is crucial for maximal sensitivity from these very large molecular weight systems. We also show results which confirm some predictions regarding the superiority of TROSY at 900 MHz vs. 800 MHz especially as the molecular weights become very large.
Triple resonance three-dimensional protein NMR: Before it became a black box.
Triple resonance three-dimensional protein NMR: Before it became a black box.
Triple resonance three-dimensional protein NMR: Before it became a black box.
J Magn Reson. 2011 Aug 30;
Authors: Bax A
Abstract
Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with (13)C and (15)N, and establishes the scalar connectivity pathway between nuclei through the large (1)J(NH), (1)J(CH)(, 1)J(CC), and (1)J(CN)...
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Triple resonance three-dimensional protein NMR: Before it became a black box
Triple resonance three-dimensional protein NMR: Before it became a black box
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 31 August 2011</br>
Ad, Bax</br>
Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with 13C and 15N, and establishes the scalar connectivity pathway between nuclei through the large 1JNH, 1JCH, 1JCC, and 1JCN couplings. The magnetization transfer process takes place...
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08-31-2011 07:12 PM
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
Fast and accurate algorithm for the simulation of NMR spectra of large spin systems.
Fast and accurate algorithm for the simulation of NMR spectra of large spin systems.
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 , which obviously does not...
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07-23-2011 08:54 AM
[NMR paper] Double and triple resonance NMR methods for protein assignment.
Double and triple resonance NMR methods for protein assignment.
Related Articles Double and triple resonance NMR methods for protein assignment.
Methods Mol Biol. 1997;60:29-52
Authors: Whitehead B, Craven CJ, Waltho JP
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08-22-2010 03:31 PM
[NMR paper] Double and triple resonance NMR methods for protein assignment.
Double and triple resonance NMR methods for protein assignment.
Related Articles Double and triple resonance NMR methods for protein assignment.
Methods Mol Biol. 1997;60:29-52
Authors: Whitehead B, Craven CJ, Waltho JP
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08-22-2010 03:03 PM
HNCB Triple Resonance Experiment (Varian)
Hello,
Has anyone come across this experiment? I see it listed but have not been able to find the pulse sequence. I have noticed that in some cases that the reference simply implies the HNCACB experiment running in such a way to allow complete transfer to the CB.
So is there an HNCB or is the only HNCB in the form of the HNCACB with the delay set to allow complete transfer to the CB?
Thanks in advance!!!