Related Experiment Video
Updated: Jul 5, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins
Wolfgang Bermel1, Ivano Bertini, Isabella C Felli
1Bruker BioSpin GmbH, Rheinstetten, Germany.
Abstract:
Natively unfolded proteins are increasingly recognized to play important physiological roles. These proteins do not crystallize, so NMR is the only technique able to provide structural and dynamic information. However, in unfolded proteins, the proton chemical shift dispersion is poor, causing severe problems in resonance assignment. We designed a novel strategy based on two protonless experiments, a CBCACON-IPAP and a novel COCON-IPAP, that permits a straightforward and unequivocal backbone heteronuclear assignment of the natively unfolded protein alpha-synuclein.
Related Concept Videos
Nuclear Magnetic Resonance (NMR): Overview
NMR spectroscopy generates a spectrum where the characteristic absorption frequencies of the sample are...
¹H NMR: Complex Splitting
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied first.
Atomic Nuclei: Magnetic Resonance
NMR Spectrometers: Radiofrequency Pulses and Pulse Sequences
Applications Of NMR In Biology
The...
Insensitive Nuclei Enhanced by Polarization Transfer (INEPT)

