To circumvent the problem of spectral congestion and provide general and non-perturbative probes of protein electrostatics and dynamics, we have been developing the use of site-selectively incorporated carbon-deuterium (C-D) bonds, which have environmentally sensitive IR absorptions in an otherwise transparent region of the protein's IR spectrum. In addition to providing high structural resolution, the C-D probes inherently provide the high time resolution sufficient for the detection and resolution of even the most rapidly interconverting species. The use of C-D bonds to characterize the electrostatics, dynamics, and folding of cytochrome c, an SH3 domain, as well as ubiquitin and dibiquitin will be discussed. In addition, to demonstrate the potential of the technique, we will show how it may be used in conjunction with biochemistry, microbiology, and genetics to provide novel insights into the evolution of new protein function in the enzyme dihydrofolate reductase.

C-D bonds as IR probes of protein electrostatics, dynamics, folding, and their application to understand the evolution of novel protein function

246th National Meeting (2013)

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