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 …

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 …

In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that
depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here …

We describe magic-angle spinning NMR experiments designed to elucidate the interstrand
architecture of amyloid fibrils. Three methods are introduced for this purpose, two being …

Solid-state nuclear magnetic resonance (ssNMR) is indispensable for studying the
structures, dynamics, and interactions of insoluble proteins in native or native-like …

Biological magic angle spinning (MAS) solid-state nuclear magnetic resonance
spectroscopy has developed rapidly over the past two decades. For the structure …

We show here that by combining tailored approaches based on ultrafast (60 kHz) MAS on
the CoII-replaced catalytic domain of matrix metalloproteinase 12 (CoMMP-12) we can …

Nanometer-range distances are important for restraining the three-dimensional structure
and oligomeric assembly of proteins and other biological molecules. Solid-state NMR …

Solid-state nuclear magnetic resonance (NMR) is a potent tool for studying the structures
and dynamics of insoluble proteins. It starts with signal assignment through multi …

Recent progress in multi-dimensional solid-state NMR correlation spectroscopy at high static
magnetic fields and ultra-fast magic-angle spinning is discussed. A focus of the review is on …