Probing Protein-Salt Interactions with Microfluidics and Nonlinear Optics

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The Analytical and Surface Chemistry (ASC) program of the Division of Chemistry will support the research program of Prof. Paul Cremer of Texas A&M University. Prof. Cremer and his students will study the fundamental mechanisms of the interactions of salts with model polypeptide systems. The study will reveal the profound effects that salts have on the physical properties of proteins. These interactions play crucial role in many processes including protein folding, enzyme turnover and supramolecular ordering. The study will involve the use of a wide variety of analysis tools including vibrational sum frequency spectroscopy (VSFS) and a novel temperature gradient microfluidic device which was developed by Prof. Cremer and his students. The study will provide an excellent educational opportunity for graduate students and postdoctoral trainees to carry out a fundamental protein dynamics study using state of the art analytical techniques. The study will be applicable to a wide variety of problems ranging from polymer physics and medicine to colloid chemistry and protein isolation.