New Problems for Solid State NMR in Molecular Biophysics
My lab develops new methods for NMR studies of biomolecular systems and applies them to a variety of problems, often in combination with electron microscopy and other techniques. This seminar will focus on two recent projects: (1) Time-resolved NMR measurements with millisecond time resolution, based on novel equipment for rapid mixing, rapid temperature jumps, rapid freezing, and ultra-low-temperature
solid state NMR. Results from studies of protein folding and amyloid-β peptide oligomerization will be presented; (2) A new approach to NMR studies of nanopore-confined peptides and proteins, based on nanoporous anodic aluminum oxide (AAO) and surface attachment through phosphonic acid/aluminum oxide chemistry. These studies aim to elucidate how nanopore confinement affects the conformations, dynamics, and interactions of intrinsically disordered FG-repeat protein sequences, which fill the central channels of nuclear pore complexes in eukaryotic cells.
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For any questions, please contact Hyacinth Camillieri at hcamillier@gc.cuny.edu