{"id":159,"date":"2026-02-16T10:56:07","date_gmt":"2026-02-16T18:56:07","guid":{"rendered":"https:\/\/dornsife.usc.edu\/wilson-lab\/?page_id=159"},"modified":"2026-02-17T11:17:14","modified_gmt":"2026-02-17T19:17:14","slug":"research","status":"publish","type":"page","link":"https:\/\/dornsife.usc.edu\/wilson-lab\/research\/","title":{"rendered":"Research"},"content":{"rendered":" \n \n\n\n\n\n\n\n\n
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\n Building tools to study biology and chemistry at the fundamental level\n <\/h2>\n\n\n<\/div>\n \n \n
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We develop magnetic resonance tools and methods to study out-of-equilibrium, dynamically evolving molecular and biophysical processes. We combine nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), and dynamic nuclear polarization (DNP) to study disease mechanisms and inform targeted drug discovery, probe interactions between proteins and nucleic acids, aid in the development and characterization of self-assembling and self-healing materials, and explore fundamental questions in chemistry, biology, and condensed matter physics.<\/p>\n\n\n\n<\/div>\n \n\n <\/div><\/div>\n\n\n\n \n \n\n\n\n\n\n\n\n

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\n Solid-State Magnetic Resonance\n <\/h2>\n\n\n<\/div>\n \n \n
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Solid-state nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), and dynamic nuclear polarization (DNP) are powerful, complementary spectroscopic techniques used to probe the structure and dynamics of materials at the atomic level.<\/p>\n

Solid-state NMR provides detailed information about local chemical environments, molecular structure, and dynamics in non-crystalline systems such as polymers, biomaterials, and heterogeneous catalysts, often using magic-angle spinning (MAS) to achieve high resolution.<\/p>\n

EPR, in contrast, specifically detects unpaired electrons, making it uniquely suited for studying paramagnetic species, radicals, transition metal centers, and defects in solids.<\/p>\n

Dynamic nuclear polarization enhances the inherently low sensitivity of NMR by transferring polarization from highly polarized electron spins to nearby nuclei under microwave irradiation. Together, these techniques offer a powerful toolkit for investigating complex solid materials, combining structural resolution, electronic insight, and enhanced sensitivity.<\/p>\n\n\n\n<\/div>\n \n <\/div>\n\n

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\n Time-Resolved Biomolecular Structures\n <\/h2>\n\n\n<\/div>\n \n \n
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Time-resolved solid-state NMR is a powerful approach for monitoring structural and dynamic changes in materials as they occur, providing molecular-level insight into processes that evolve over time. By acquiring a series of NMR spectra during a reaction, phase transition, crystallization, adsorption event, or mechanical transformation, we enable direct observation of transient intermediates, kinetic pathways, and evolving local environments.<\/p>\n

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\n Biomolecular interactions underlying neurodegenerative diseases\n <\/h2>\n\n\n<\/div>\n \n \n
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Amyloid fibril\u2013forming proteins are a class of proteins that can self-assemble into highly ordered, \u03b2-sheet\u2013rich fibrillar aggregates known as amyloids. Many are associated with pathological processes, particularly in neurodegenerative diseases. In disorders such as Alzheimer\u2019s disease, Parkinson\u2019s disease, and amyotrophic lateral sclerosis (ALS), specific proteins self-assemble into insoluble fibrils that accumulate in the brain. These aggregates can disrupt cellular function, impair proteostasis, and trigger inflammation, ultimately contributing to neuronal dysfunction and cell death.<\/p>\n

We apply novel magnetic resonance methods to probe the structural and mechanistic basis of amyloid formation, in order to understand the molecular self-assembly process at a fundamental level. The ultimate goal is to shed light on disease progression and inform therapeutic strategies.<\/p>\n\n\n\n<\/div>\n \n <\/div>\n\n

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