title: Sensitivity-enhanced IPAP-SOFAST-HMQC for fast-pulsing 2D NMR with reduced radiofrequency load.
abstract: The SOFAST-HMQC experiment [P. Schanda, B. Brutscher, Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds, J. Am. Chem. Soc. 127 (2005) 8014-8015] allows recording two-dimensional correlation spectra of macromolecules such as proteins in only a few seconds acquisition time. To achieve the highest possible sensitivity, SOFAST-HMQC experiments are preferably performed on high-field NMR spectrometers equipped with cryogenically cooled probes. The duty cycle of over 80% in fast-pulsing SOFAST-HMQC experiments, however, may cause problems when using a cryogenic probe. Here we introduce SE-IPAP-SOFAST-HMQC, a new pulse sequence that provides comparable sensitivity to standard SOFAST-HMQC, while avoiding heteronuclear decoupling during (1)H detection, and thus significantly reducing the radiofrequency load of the probe during the experiment. The experiment is also attractive for fast and sensitive measurement of heteronuclear one-bond spin coupling constants.
authors: Laboratoire de RMN, Institut de Biologie Structurale Jean-Pierre Ebel, CEA/Centre National de la Recherche Scientifique, UJF, 41 rue Jules Horowitz, Grenoble Cedex, France.
authors: Thomas
authors: T
authors: Kern
authors: Paul
authors: P
authors: Schanda
authors: Bernhard
authors: B
authors: Brutscher
mesh_terms: D006859:Hydrogen; D007768:Lactalbumin / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D009587:Nitrogen Isotopes; D011506:Proteins; D025801:Ubiquitin; D006859:Hydrogen; D007768:Lactalbumin