Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and
neurites, hallmarks of Parkinson's disease (PD). We present a high-resolution structure of an …

Protein structure determination methods using magic-angle spinning solid-state nuclear
magnetic resonance (MAS SSNMR) have experienced a remarkable development in the …

For over 50 years, amphotericin has remained the powerful but highly toxic last line of
defense in treating life-threatening fungal infections in humans with minimal development of …

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 …

α-Synuclein (AS) fibrils are the major component of Lewy bodies, the pathological hallmark
of Parkinson's disease (PD). Here, we use results from an extensive investigation employing …

α-Synuclein (AS) fibrils are the main protein component of Lewy bodies, the pathological
hallmark of Parkinson's disease and other related disorders. AS forms helices that bind …

The function of a protein is predicated upon its three-dimensional fold. Representing its
complex structure as a series of repeating secondary structural elements is one of the most …

α-Synuclein (AS) is associated with both sporadic and familial forms of Parkinson disease
(PD). In sporadic disease, wild-type AS fibrillates and accumulates as Lewy bodies within …

Dynamic nuclear polarization of 17O was studied using four different polarizing agents: the
biradical TOTAPOL and the monoradicals trityl and SA-BDPA, as well as a mixture of the …

Two fluorescence-tagged carbohydrate-binding modules (CBMs), which specifically bind to
crystalline (CBM2a-RRedX) and paracrystalline (CBM17-FITC) cellulose, were used to …