RUI: Solubility and Dynamic Implications for Structurally Homologous Disaccharides

在化学系化学结构，动力学和机制A（CSDM-A）计划的支持下，来自Ripon学院的Christina Othon沿着来自Ripon学院的帕特里克威洛比和来自卫斯理大学的Erika Taylor将使用实验和计算方法来研究二糖在溶液中的稳定性。二糖的水合和动力学性质影响这些分子如何稳定蛋白质。Othon博士和她的团队将整合分子动力学模拟，生物物理测定和超快光谱学来研究溶液中葡萄糖基二糖的水合和动力学性质，以便了解对溶解度，氢键能力以及分子赋予溶剂的能量和动力学变化的影响。本科生和研究生将在这些研究活动中接受培训，这将通过课程培训模块和研讨会活动的开发得到补充。溶剂介导的渗透稳定蛋白质的直接证据对于了解热和其他环境应力波动如何影响这些重要生物大分子的稳定性和功能非常重要。计算对接模型，圆二色性，量热测量将被用来研究如何二糖和它们的立体异构体在他们的能力不同，以稳定蛋白质结构。然后将使用超快荧光频率上转换光谱法评估水合动力学。这种组合和计算和实验方法预计将导致在分子水平上的理解有关的蛋白质溶质和溶质诱导的溶剂修饰的渗透剂stabilization.This奖反映了NSF的法定使命的优先溶剂化模型，并已被认为是值得通过使用基金会的智力价值和更广泛的影响审查标准进行评估的支持。

With support from the Chemical Structure, Dynamics, and Mechanisms A (CSDM-A) Program in the Division of Chemistry, Christina Othon from Ripon College along with Patrick Willoughby from Ripon College and Erika Taylor from Wesleyan University will use both experiments and computational methods to study the stability of disaccharides in solution. The hydration and dynamical properties of disaccharides impact how these molecules stabilize proteins. Dr. Othon and her team will integrate molecular dynamics simulations, biophysical assays, and ultrafast spectroscopy to study the hydration and dynamical properties of glucose-based disaccharides in solution so that impacts on solubility, hydrogen bonding capacity, and the energetic and kinetic changes the molecules impart to the solvent can be learned. Undergraduate and graduate students will be trained in these research activities and this will be supplemented by the development of coursework training modules and workshop activities.Direct evidence of solvent-mediated osmolyte stabilization of proteins is important for understanding how thermal and other environmental stress fluctuations influence the stability and function of these important biomacromolecules. Computational docking models, circular dichroism, and calorimetry measurements will be used to investigate how disaccharides and their stereoisomers differ in their ability to stabilize protein structure. Hydration dynamics will then be evaluated using ultrafast fluorescence frequency up-conversion spectroscopy. This combination and computational and experimental approaches are expected to result in a molecular level understanding of the preferential solvation model regarding relevant protein-solute and solute-induced solvent modification for osmolyte stabilization.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.