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Creators/Authors contains: "Sharp, Joshua S"

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  1. ; ; ; ; ; ; ; ; ; ; et al (, ACS Nano)
    Free, publicly-accessible full text available November 5, 2025
  2. ; ; ; ; ; ; ; (, Materials Chemistry Frontiers)
    Schematic representation of preferential uptake of good's buffer-coated PLGA nanoparticles into human breast cancer cells. Created with biorender.com. 
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    Full Text Available 
  3. ; ; ; ; ; ; ; ; ; ; et al (, Journal of Natural Products)
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  4. ; ; ; ; ; ; ; ; ; ; et al (, Communications Biology)
    Abstract High resolution hydroxyl radical protein footprinting (HR-HRPF) is a mass spectrometry-based method that measures the solvent exposure of multiple amino acids in a single experiment, offering constraints for experimentally informed computational modeling. HR-HRPF-based modeling has previously been used to accurately model the structure of proteins of known structure, but the technique has never been used to determine the structure of a protein of unknown structure. Here, we present the use of HR-HRPF-based modeling to determine the structure of the Ig-like domain of NRG1, a protein with no close homolog of known structure. Independent determination of the protein structure by both HR-HRPF-based modeling and heteronuclear NMR was carried out, with results compared only after both processes were complete. The HR-HRPF-based model was highly similar to the lowest energy NMR model, with a backbone RMSD of 1.6 Å. To our knowledge, this is the first use of HR-HRPF-based modeling to determine a previously uncharacterized protein structure. 
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