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Updated: Aug 8, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Excitation of selected proton signals in NMR of isotopically labeled macromolecules
Pelupessy1, Chiarparin, Bodenhausen
1Section de Chimie, Universite de Lausanne, Lausanne, 1015, Switzerland.
Abstract:
In isotopically labeled macromolecules, it is possible to excite the signal of a selected proton by shuttling magnetization back and forth between the chosen proton and a heteronucleus such as 13C or 15N, using two-way doubly selective heteronuclear cross-polarization. Selective excitation of a chosen proton can be followed by homonuclear coherence transfer to identify side-chain resonances of the corresponding amino acid in proteins. The resulting one-dimensional experiments yield information that can usually only be obtained from three-dimensional HSQC-TOCSY spectra. The method also provides efficient suppression of solvent signals without affecting resonances close to the solvent peak. Copyright 1999 Academic Press.
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