Characterization of protein molecular recognition is challenged by both the spatial heterogeneity of proteins and the rapid interconversion of potentially important conformational states.  Our group combines the inherent temporal resolution of linear and two-dimensional infrared spectroscopy with the spatial resolution afforded by site-selective incorporation of vibrational reporter groups that provide frequency-resolved absorptions to characterize changes in local environments in proteins.   I will present our application of this approach for characterizing fast side chain dynamics in the recognition of Src homology 3 domains to proline-rich motifs and plastocyanin to cytochrome <i>f</i>. <br/>

Conformations and dynamics of protein molecular recognition via 2D IR spectroscopy

253rd National Meeting (2017)

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