Although protein dynamics are increasingly evoked as contributors to protein function, rigorous experimental assessment of their role has been challenged by both the spatial heterogeneity of proteins and the rapid interconversion of potentially important conformational states.  We are combining the inherent high temporal resolution of linear FT and 2D infrared (IR) spectroscopy with the spatial resolution afforded by site-selective incorporation of vibrational reporter groups via protein engineering to generate the highest resolution picture possible of the conformational dynamics involved in protein function.  To improve this approach, we are exploring new IR potential IR probes of proteins to extend the dynamic range.  These probes are being applied to study the binding-induced changes in dynamics along the interaction interface between electron transfer partners plastocyanin and cytochrome <i>f</i>.<br/>

Site-specific dynamics of protein molecular recognition via 2D IR spectroscopy

251st National Meeting (2016)

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