Related ArticlesImproving NMR sensitivity in room temperature and cooled probes with dipolar ions.
J Magn Reson. 2005 Apr;173(2):339-43
Authors: Lane AN, Arumugam S
The response of inverse triple resonance cold and conventional probes to ionic strength has been compared under a variety of conditions relevant to protein NMR. Increasing the salt concentration degrades probe performance in terms of sensitivity, and the effect is more severe for cold probes and with increasing magnetic field strength. This is especially noticeable for experiments that involve a spin lock or decoupling, where sensitivity losses compared with pure water can be more than 2-fold. We have investigated the use of glycine as a substitute for salt as a supporting solute for proteins, and we show that it has a minimal effect on probe tuning or performance. Readily available d5-Gly is a useful co-solute for protein NMR, especially at high magnetic field strengths and on cold probes, as it maintains solubility while not degrading probe performance.
[NMR paper] Sensitivity of NMR residual dipolar couplings to perturbations in folded and denature
Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease.
Related Articles Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease.
Biochemistry. 2005 May 3;44(17):6392-403
Authors: Sallum CO, Martel DM, Fournier RS, Matousek WM, Alexandrescu AT
The invariance of NMR residual dipolar couplings (RDCs) in denatured forms of staphylococcal nuclease to changes in denaturant concentration or amino acid sequence has previously been attributed...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] High-sensitivity observation of dipolar exchange and NOEs between exchangeable proton
High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
Related Articles High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy.
J Am Chem Soc. 2003 Nov 26;125(47):14222-3
Authors: Paulson EK, Morcombe CR, Gaponenko V, Dancheck B, Byrd RA, Zilm KW
A highly sensitive new 1H-detected 3D solid-state NMR method is described for characterizing 1H-1H spin exchange in nanocrystalline samples of...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] The importance of being ordered: improving NMR structures using residual dipolar coup
The importance of being ordered: improving NMR structures using residual dipolar couplings.
Related Articles The importance of being ordered: improving NMR structures using residual dipolar couplings.
C R Biol. 2002 Sep;325(9):957-66
Authors: Gronenborn AM
Residual dipolar couplings arise from small degrees of alignment of molecules in a magnetic field. Most biomolecules lack sufficient intrinsic magnetic susceptibility anisotropies for practical purposes; however, alignment can be achieved using dilute aqueous phospholipid mixtures, colloidal...