In the Spring of 2013, NMR spectroscopists convened at the Weizmann Institute in Israel to
brainstorm on approaches to improve the sensitivity of NMR experiments, particularly when …

Solid‐state NMR spectroscopy is an emerging tool for structural studies of crystalline,
membrane‐associated, sedimented, and fibrillar proteins. A major limitation for many studies …

We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid‐
state NMR spectroscopy with 100–111 kHz magic‐angle spinning (MAS). The excellent …

Im Frühling 2013 versammelten sich NMR‐Spektroskopiker am Weizmann‐Institut in Israel,
um neue Ansätze zur Verbesserung der Empfindlichkeit von NMR‐Experimenten zu …

Solution-state nuclear magnetic resonance (NMR) spectroscopy is a very successful method
to characterize the structure and dynamics of biomolecules in solution.[1, 2] However …

Understanding the dynamics of interacting proteins is a crucial step toward describing many
biophysical processes. Here we investigate the backbone dynamics for protein GB1 in two …

Chromatin function depends on a dense network of interactions between nucleosomes and
a wide range of proteins. A detailed description of these protein–nucleosome interactions is …

Co‐translational protein folding is not yet well understood despite the availability of high‐
resolution ribosome crystal structures. We present first solid‐state NMR data on non‐mobile …

Protein–nucleic acid interactions play important roles not only in energy‐providing reactions,
such as ATP hydrolysis, but also in reading, extending, packaging, or repairing genomes …

Abstract Structure determination of adjuvant‐coupled antigens is essential for rational
vaccine development but has so far been hampered by the relatively low antigen content in …