Solvation Shell Structure of Small Molecules and Proteins by IR-MCR Spectroscopy.

The flexibility of the hydrogen-bonded network of water is the basis for its excellent solvation properties. Accordingly, it is valuable to understand the properties of water in the solvation shell surrounding small molecules and biomolecules. Recent high-quality Raman spectra analyzed with Self-Modeling Curve Resolution (SMCR) have provided Raman spectra of small-molecule solvation shells. Here we apply SMCR to the complementary technique of Fourier transform infrared (FTIR) spectroscopy in the attenuated total reflection (ATR) configuration to extract the IR spectra of solvation shells. We first illustrate the method by obtaining the IR-MCR solvation shell spectra of tert-butanol (TBA), before applying it to antifreeze protein type III. Our results show that IR-SMCR spectroscopy is a powerful method for studying the solvation shell structure of small molecules and biomolecules. Given the wide availability of FTIR-ATR instruments, the method could prove to be an impactful tool for studying solvation and solvent-mediated interactions.