H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.
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.
Bermel
Wolfgang
W
Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten, Germany.
Bertini
Ivano
I
Csizmok
Veronika
V
Felli
Isabella C
IC
Pierattelli
Roberta
R
Tompa
Peter
P
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
D002247:Carbon Isotopes; D009363:Neoplasm Proteins; D009590:Nitrogen Radioisotopes; D011506:Proteins; D064249:Securin; C578002:pituitary tumor-transforming protein 1, human; D006859:Hydrogen