title: H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.
abstract: Here, we present a series of exclusively heteronuclear multidimensional NMR experiments, based on 13C direct detection, which exploit the (1)H polarization as a starting source to increase the signal-to-noise ratio. This contributes to make this spectroscopy more useful and usable. Examples are reported for a suitable system such as securin, an intrinsically disordered protein of 22 kDa.
authors.affiliation: Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Bermel
authors.forename: Ivano
authors.initials: I
authors.lastname: Bertini
authors.forename: Veronika
authors.initials: V
authors.lastname: Csizmok
authors.forename: Isabella C
authors.initials: IC
authors.lastname: Felli
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
authors.forename: Peter
authors.initials: P
authors.lastname: Tompa
mesh_terms: D000465:Algorithms; D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen / Q000737:chemistry*; D009363:Neoplasm Proteins / Q000737:chemistry; D009590:Nitrogen Radioisotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D050050:Protein Carbonylation; D011506:Proteins / Q000737:chemistry*; D064249:Securin
chemical_list: D002247:Carbon Isotopes; D009363:Neoplasm Proteins; D009590:Nitrogen Radioisotopes; D011506:Proteins; D064249:Securin; C578002:pituitary tumor-transforming protein 1, human; D006859:Hydrogen