15N-correlated three-dimensional relayed NOESY experiments in uniformly 15N-labeled proteins
β Scribed by Luciano Mueller; Sharon Campbell-Burk; Peter Domaille
- Publisher
- Elsevier Science
- Year
- 1992
- Weight
- 556 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0022-2364
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π SIMILAR VOLUMES
The precision of a protein structure determined by NMR spectroscopy is strongly influenced by the number of longrange NOE interactions per residue. Aromatic and methylcontaining residues are frequently located in the hydrophobic interior of proteins and yield long-range NOE interactions. Methyl grou
A number of heteronuclear 3D techniques have been de-constant-time period of 26-28 ms [2l / 2T(CO)] follows, veloped in recent years to obtain the complete assignment which allows optimum refocusing of the Ca, Cb coupling of 15 N, 13 C-labeled proteins (1). An experiment that often and also allows t
A novel method for suppression of diagonal peaks in the amide region of NOESY NMR spectra of 15 N-labeled proteins is presented. The method is particularly useful for larger proteins at high magnetic fields where interference between dipolar and chemical shift anisotropy relaxation mechanisms result