Controlling and Probing the Microscopic Structure and Dynamics of Liquids

在这项由化学学部实验物理化学项目资助的教师早期职业发展奖中，波士顿学院的John Fourkas将使用超快非线性光学技术来探测纯液体和溶液中的分子间相互作用，这些液体和溶液受到微孔玻璃的限制或保持在持续张力的非平衡状态。瞬态光栅光学克尔效应研究将探测这些系统中的重定向扩散速率，提供有关液体局部结构的信息。这种结构对吸引力（如氢键）和疏水力（如离子溶质引起的疏水力）很敏感。这些力参与了各种各样的过程，包括蛋白质折叠和气泡合并。该计划的教育部分包括设计一个拓展计划，在学校提供科学演示，为小学教师提供研讨会，设计涉及当代研究问题的本科化学实验，并在研究生课程中开发沟通技巧课程。液体中分子的局部组织，特别是水，是许多固相性质的原因。氢键等作用力对分子溶解在水中时的行为有很大的影响。富尔卡斯教授将研究这些力的性质以及溶解分子对这种局部秩序的影响。这些研究将提供可应用于诸如理解蛋白质折叠和分子与酶结合等领域的信息。

In this Faculty Early Career Development Award funded by the Experimental Physical Chemistry Program in the Chemistry Division, John Fourkas of Boston College will use ultrafast nonlinear optical techniques to probe intermolecular interactions in pure liquids and solutions subjected to confinement in microporous glasses or maintained in a non-equilibrium state of sustained tension. Transient Grating Optical Kerr Effect studies will probe the reorientational diffusion rates in these systems, providing information on the local structure of the liquid. This structure will be sensitive to attractive forces such as hydrogen bonding and hydrophobic forces such as those caused by ionic solutes. These forces are involved in a wide variety of processes including protein folding and bubble coalescence. The educational component of this program involves designing an outreach program to provide science demonstrations at schools and seminars for grade school teachers, designing undergraduate chemistry experiments involving contemporary research problems, and developing courses in communications skills in the graduate curriculum. The local organization of molecules in liquids, water in particular, is responsible for many solution phase properties. Forces such as hydrogen bonding have a large impact on the way molecules behave when dissolved in water. Professor Fourkas will study the nature of these forces and the effects that dissolved molecules have on this local order. These studies will provide information which can be applied to areas such as understanding protein folding and the binding of molecules to enzymes.