Hydrogen/deuterium (H/D) exchange in proteins is useful to study structures and dynamics of proteins, providing information about solvent accessibility at protein surfaces. Although H/D exchange can be studied by NMR, mass spectrometry and FTIR in bulk solutions, not much progress has been made for studying proteins at interfaces due to a lack of surface-selective methods. Here, we introduce chiral sum frequency generation (SFG) spectroscopy as a new approach to probe H/D exchange in proteins at interfaces. We demonstrate that changes in the N-H/N-D stretch signals in chiral SFG spectra can reveal the kinetics of H/D exchange in protein in situ and in real time. The major advantage of this method is zero background from the O-H stretch of water. Further applications are expected to address fundamental questions related to solvent-protein interactions on membrane surfaces, proton transfer in membrane proteins, and intramolecular hydrogen bonding interactions of proteins associated with membrane.

Chiral sum frequency generation spectroscopy for probing the hydrogen/deuterium exchange in proteins at interfaces

244th National Meeting (2012)

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