Abstract
Advances in protein two-dimensional infrared spectroscopy and computational spectroscopy of amide I vibrations have provided a way to characterize the conformational variation and disorder in protein structure. These techniques use isotope-edited amide I spectra in combination with spectra computed from Markov state models built from molecular dynamics simulations to infer variation in local configuration and to refine ensembles for peptides and proteins. This talk will describe these tools drawing on examples from studies of insulin monomer and dimer structure and the dynamic interactions in the monomer-dimer equilibrium.
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