Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …

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 …

Nuclear Magnetic Resonance (NMR) spectroscopy is a well-established method for the
investigation of various types of porous materials. During the past decade, metal–organic …

In recent years, exciting developments in instrument technology and experimental
methodology have advanced the field of magic-angle spinning (MAS) nuclear magnetic …

Solid-state nuclear magnetic resonance (NMR) spectroscopy has matured to the point that it
is possible to determine the structure of proteins in immobilized states, such as within …

Using deuteron spin-lattice and spin-spin relaxometry, the reorientational dynamics of
ethaline (choline chloride/ethylene glycol) and reline (choline chloride/urea) are studied in a …

Proteins are dynamic entities and populate ensembles of conformations. Transitions
between states within a conformational ensemble occur over a broad spectrum of amplitude …

We demonstrate the determination of quantitative rates of molecular reorientation in the solid
state with rotating frame (R1ρ) relaxation measurements. Reorientation of the carbon …

We show that ultra-wideline solid-state 14N NMR can be used as a quantitative probe of
molecular dynamics. Jump rates for the molecular flipping mechanism in crystalline urea are …

Based on continuous methodical advances and developments, solid-state NMR
spectroscopy has become a powerful tool for the investigation of various materials, including …