Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

Magic angle spinning (MAS) nuclear magnetic resonance (NMR) has evolved significantly
over the past three decades and established itself as a vital tool for the structural analysis of …

The microtubule-associated protein tau aggregates into neurofibrillary tangles in Alzheimer's
disease (AD). The main type of aggregates, the paired helical filaments (PHF), incorporate …

Determination of structure of integral membrane proteins, especially in their native
environment, is a formidable challenge in structural biology. Here we demonstrate that …

Abstract β-barrel proteins mediate nutrient uptake in bacteria and serve vital functions in cell
signaling and adhesion. For the 14-strand outer membrane protein G of Escherichia coli …

COVID-19 has accounted for more than 6 million deaths worldwide. Bacillus Calmette–
Guérin (BCG), the existing tuberculosis vaccine, is known to induce heterologous effects …

The amyloid fold is structurally characterized by a typical cross-β architecture, which is under
debate to represent an energy-favourable folding state that many globular or natively …

Neurodegenerative disorders are frequently associated with β-sheet-rich amyloid deposits.
Amyloid-forming proteins can aggregate under different structural conformations known as …

TA (toxin–antitoxin) systems are widely distributed amongst bacteria and are associated with
the formation of antibiotic tolerant (persister) cells that may have involvement in chronic and …

Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and
infectious state correspond to conformational transition of a protein fold. The conformational …