Probing Protein-Salt Interactions with Microfluidics and Nonlinear Optics

化学系的分析和表面化学(ASC)计划将支持德克萨斯农工大学保罗·克里默教授的研究计划。克里默教授和他的学生将研究盐与模型多肽系统相互作用的基本机制。这项研究将揭示盐对蛋白质物理性质的深刻影响。这些相互作用在蛋白质折叠、酶的周转和超分子有序等过程中起着至关重要的作用。这项研究将涉及到各种分析工具的使用，包括振动和频谱(VSFS)和由Cremer教授和他的学生开发的新型温度梯度微流控装置。这项研究将为研究生和博士后实习生提供一个很好的教育机会，让他们使用最先进的分析技术进行基础蛋白质动力学研究。这项研究将适用于从聚合物物理和医学到胶体化学和蛋白质分离的广泛问题。

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.