Owen A. Warmuth

The paper reports the high-resolution SSNMR structure of A30P mutant alpha-synuclein fibrils, showing a conserved Greek key fold not including the mutation site, and validates a method for comparing SSNMR spectra of Asyn polymorphs.

The paper reports the high-resolution structure of protonated EmrE, revealing how the C-terminal tail occludes the transport pore to prevent proton leak.

This paper introduces ANSA, an automated NMR spectral alignment tool using cryo-EM motion correction, improving alignment accuracy and reducing manual effort in NMR data processing.

The paper reports high-resolution 13C and 15N backbone chemical shift assignments for Toho-1 β-lactamase using advanced solid-state NMR techniques, confirming conserved secondary structure.

This study improves solid-state NMR resolution for high molecular weight proteins using GHz-class spectrometers and novel techniques, achieving better than 0.2 ppm resolution for proteins up to 144 kDa.

The paper classifies Alpha-synuclein fibril structures into two main polymorph classes using clustering and finds conserved motifs that could guide drug design.

This study determines the atomic structure of alpha-synuclein fibrils from Lewy body dementia tissue using a novel amplification method and solid-state NMR.