15N HSQC with Real Time Acquisition Pure Shift for Proteins

This pulse sequence version is obsolete (Oct, 2017).
New version is available.

Pure Shift NMR Spectroscopy suppresses the effects of homonuclear coupling, allowing HSQC spectra to be produced that contain chemical shift information only in both dimensions. Where homonuclear couplings are resolved in the proton dimension of a standard HSQC spectrum, pure shift methods can improve both resolution and sensitivity. Unlike the standard PS gHSQC sequence, the pulse sequences below can be used even in the presence of strong non-deuterated solvent signals (e.g. 90% H2O/10% D2O). Pulse sequences and example data are available for real-time BIRD and band-selective methods, implemented on Varian/Agilent and Bruker spectrometers.


Pulse Sequence packages:
rtPS-gHSQC_protein_JBN pulse sequence zip file (right click and chose 'save ... as')
Parameter file zip (right click and chose 'save ... as')
Example data set zip (right click and chose 'save ... as')

Pulse sequence using Band-selective Homodecoupling (BASHD): rtPS_gHSQCgBASHD (right click and chose 'save ... as')
Pulse sequence using BIRD rtPS_gHSQCgBIRD (right click and chose 'save ... as')
Reference pulse sequence (without homodecoupling) rtPS_gHSQCref (right click and chose 'save ... as')

Real-time pure shift N-15 HSQC of proteins: a real improvement in resolution and sensitivity
Kiraly, P.; Adams, R.W.; Paudel, L.; Foroozandeh, M.; Aguilar, J.A.; Timari, I.; Cliff, M.J.; Nilsson, M.; Sandor, P.; Batta, G.; Waltho, J.P.; Kover, K.E.; Morris, G.A.
J. Biomol. NMR 2015, 62, 43-52