Publications by authors named "Owen Warmuth"
Article Synopsis
- Amyloid fibrils are protein structures associated with neurodegenerative diseases, and they are important for creating specific ligands for medical imaging and treatment.
- Solid-state NMR (SSNMR) is a technique used to analyze these fibrils, but traditional methods require a lot of manual data analysis, which slows down the process.
- The study presents a new automated method using probabilistic assignment and symmetry in software, which successfully determined the structure of an α-synuclein fibril linked to Parkinson's, significantly reducing the time and manual effort needed for structure analysis.
Magic-angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) spectroscopy is a powerful and versatile technique for probing structure and dynamics in large, insoluble biological systems at atomic resolution. With many recent advances in instrumentation and polarization methods, technology development in SSNMR remains an active area of research and presents opportunities to further improve data collection, processing, and analysis of samples with low sensitivity and complex tertiary and quaternary structures. SSNMR spectra are often collected as multidimensional data, requiring stable experimental conditions to minimize signal fluctuations (t noise).
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- Sensitivity is crucial for NMR experiments, with the signal-to-noise ratio (SNR) generally improving as the static magnetic field strength (B) increases, contingent on the design of the NMR probe and receiver.
- In the low magnetic field limit, SNR improves by a factor of B to the power of 7/4 for small coil geometries, and this holds true for modern magic-angle spinning (MAS) configurations up to a certain size and magnetic field strength.
- A comprehensive study evaluated SNR under MAS for varying magnetic field strengths from 14.1 to 21.1 T, using different probe designs and standard samples, revealing optimal SNR configurations for different rotor sizes and magnetic fields.
Article Synopsis
- * The researchers developed a new method to enhance the extraction of these alpha-synuclein fibrils from postmortem tissue, using solid state nuclear magnetic resonance (SSNMR) to analyze their atomic structure.
- * Their findings reveal that the fibrils from Lewy body dementia consist of both single and double protofilaments, and display structural similarities to previously studied twisted fibrils; this could aid in understanding disease mechanisms and developing new treatments.
Article Synopsis
- - The main feature of Parkinson disease (PD) and Lewy body dementia (LBD) is the buildup of alpha-synuclein (Asyn) fibrils in structures known as Lewy bodies and neurites.
- - A new method was developed to amplify Asyn fibrils from postmortem LBD tissue, allowing researchers to study their atomic structure using solid state nuclear magnetic resonance (SSNMR).
- - The amplified Asyn fibrils consist of two protofilaments with a specific structural arrangement, showing similarities to a previous study, which provides insights for understanding disease mechanisms and potential treatments targeting Asyn.
Extremotolerant organisms from all domains of life produce protective intrinsically disordered proteins (IDPs) in response to desiccation stress. In vitro, many of these IDPs protect enzymes from dehydration stress better than U.S.
View Article and Find Full Text PDFWater is essential to protein structure and stability, yet our understanding of how water shapes proteins is far from thorough. Our incomplete knowledge of protein-water interactions is due in part to a long-standing technological inability to assess experimentally how water removal impacts local protein structure. It is now possible to obtain residue-level information on dehydrated protein structures via liquid-observed vapor exchange (LOVE) NMR, a solution NMR technique that quantifies the extent of hydrogen-deuterium exchange between unprotected amide protons of a dehydrated protein and DO vapor.
View Article and Find Full Text PDFProtein-based biological drugs and many industrial enzymes are unstable, making them prohibitively expensive. Some can be stabilized by formulation with excipients, but most still require low temperature storage. In search of new, more robust excipients, we turned to the tardigrade, a microscopic animal that synthesizes cytosolic abundant heat soluble (CAHS) proteins to protect its cellular components during desiccation.
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