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 …

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 …

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 …

The detection and characterization of trapped water molecules in chemical entities and
biomacromolecules remains a challenging task for solid materials. We herein present proton …

Resolution in proton solid state magic angle sample spinning (MAS) NMR is limited by the
intrinsically imperfect nature of coherent averaging induced by either MAS or multiple pulse …

Experimentally determined protein structures often feature missing domains. One example is
the C‐terminal domain (CTD) of the hepatitis B virus capsid protein, a functionally central …

Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization
of various materials, ranging from small molecules to biological samples, including …