Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids.
A novel solid-state NMR concept is introduced that allows for the detection of through-space proton-proton contacts in high spectral resolution. The proposed method not only can be utilized to infer sequential assignments and backbone or side chain conformation in solid-phase polypeptides, but it also provides information about the three-dimensional arrangement of the molecule of interest. As a result, the molecular structure can be studied without additional restrictions regarding sample labeling or magic angle spinning rates.
Lange
Adam
A
Max-Planck-Institute for Biophysical Chemistry, Solid-State NMR, Department for NMR-based Structural Biology, Am Fassberg 11, 37077 Göttingen, Germany.
Luca
Sorin
S
Baldus
Marc
M
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011522:Protons; D025801:Ubiquitin / Q000737:chemistry*
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D025801:Ubiquitin