High-Sensitivity Observation of Dipolar Exchange and NOEs between Exchangeable Protons in Proteins by 3D Solid-State NMR Spectroscopy

Abstract

A highly sensitive new 1H-detected 3D solid-state NMR method is described for characterizing 1H-1H spin exchange in nanocrystalline samples of 15N- and 2H-enriched protein. Long-range contacts are observed in human ubiquitin. The method is also used to show that numerous NOEs between backbone amides and crystal water protons can be observed.