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 …

Multiplexing NMR experiments by direct detection of multiple free induction decays (FIDs) in
a single experiment offers a dramatic increase in the spectral information content and often …

Abstract Magic-Angle Spinning (MAS) Nuclear Magnetic Resonance (NMR) is a fast-
developing technique, capable of complementing solution NMR, X-ray crystallography, and …

Solid-state NMR spectroscopy has been playing a significant role in elucidating the
structures and dynamics of materials and proteins at the atomic level for decades. As an …

Proteins are dynamic molecules, relying on conformational changes to carry out function.
Measurement of these conformational changes can provide insight into how function is …

Solid‐state NMR (ssNMR) spectroscopy has emerged as the method of choice to analyze
the structural dynamics of fibrillar, membrane‐bound, and crystalline proteins that are …

Abstract 1H-detected solid-state NMR spectroscopy has been becoming increasingly
popular for the characterization of protein structure, dynamics, and function. Recently, we …

Internuclear distance determination is the foundation for NMR-based structure calculation.
However, high-precision distance measurement is a laborious process requiring lengthy …