Real-time pure shift ¹⁵N HSQC of proteins: a real improvement in resolution and sensitivity.

ABSTRACT: Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here. Both resolution and sensitivity are improved, without any increase in experiment time. In these experiments, free induction decays are collected in short bursts of data acquisition, with durations short on the timescale of J-evolution, interspersed with suitable refocusing elements. The net effect is real-time (t 2) broadband homodecoupling, sup

SUBMITTER: Kiraly P 

PROVIDER: S-EPMC4432093 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature