Solid-state NMR spectroscopy is one of the most commonly used techniques to study the
atomic-resolution structure and dynamics of various chemical, biological, material, and …

Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

With the development of NMR methodology and technology during the past decades, solid-
state NMR (ssNMR) has become a particularly important tool for investigating structure and …

Progress in NMR in general and in biomolecular applications in particular is driven by
increasing magnetic-field strengths leading to improved resolution and sensitivity of the …

The available magnetic field strength for high resolution NMR in persistent superconducting
magnets has recently improved from 23.5 to 28 Tesla, increasing the proton resonance …

Proton detection developed in the last 20 years as the method of choice to study
biomolecules in the solid state. In perdeuterated proteins, proton dipolar interactions are …

In recent years it is shown that mechanochemical strategies can be beneficial in directed
conversions of organic compounds. Finding new reactions proved difficult, and due to the …

The NMR spectra of side-chain protons in proteins provide important information, not only
about their structure and dynamics, but also about the mechanisms that regulate interactions …