H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.

TitleH-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.
Publication TypeJournal Article
Year of Publication2009
AuthorsBermel, W., I. Bertini, V. Csizmok, I. C. Felli, R. Pierattelli, and P. Tompa
JournalJ Magn Reson
Volume198
Issue2
Pagination275-81
Date Published2009 Jun
ISSN1096-0856
KeywordsAlgorithms, Carbon Isotopes, Humans, Hydrogen, Neoplasm Proteins, Nitrogen Radioisotopes, Nuclear Magnetic Resonance, Biomolecular, Protein Carbonylation, 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.

DOI10.1016/j.jmr.2009.02.012
Alternate JournalJ. Magn. Reson.
PubMed ID19307141