NSF PostDoctoral Research Fellowship in Biology

这项行动为2008财政年度的NSF生物学博士后研究奖学金提供资金。该研究金支持Edward P.奥布莱恩的一项研究和培训计划，题为“剖析控制蛋白质聚集和淀粉样蛋白形成的解决方案力量”。这项研究的主办机构是剑桥大学，赞助科学家是克里斯托弗多布森博士。蛋白质聚集和淀粉样蛋白形成（一种有序的蛋白质聚集体）发生在动物、细菌和真菌中，并且取决于它们发生的时间和地点，它们可能对生存有害或有益。这些生物体内的细胞内和细胞外环境代表了可以促进或抑制这些聚集体形成的广泛条件（在温度、pH和渗透压物质方面）。在理解这些溶液条件支配蛋白质聚集的机制方面存在根本性的差距。这项研究正在建模和预测这种广泛的生物相关的解决方案条件对聚集的热力学和动力学的影响，并在此过程中，解剖和理解这些不同的解决方案因素发挥的作用。培训目标包括计算和理论建模，荧光和电子显微镜技术，以及增强采样。这项研究将推进普通生物学，生物物理化学，计算生物物理学，生物信息学和影响生物技术领域的知识，其中蛋白质聚集是不可取的。

This action funds an NSF Postdoctoral Research Fellowship in Biology for FY 2008. The fellowship supports a research and training plan entitled "Dissecting the solution forces governing protein aggregation and amyloid formation" for Edward P. O'Brien. The host institution for this research is the University of Cambridge and the sponsoring scientist is Dr. Christopher Dobson. Protein aggregation and amyloid formation (a type of ordered protein aggregate) occur in animals, bacteria, and fungi and can be either detrimental or beneficial to survival depending on when and where they occur. The intracellular and extracellular environments within these organisms represent a wide range of conditions (in terms of temperature, pH and osmolytes) that can either promote or suppress the formation of these aggregates. There is a fundamental gap in the understanding of the mechanisms by which these solution conditions govern protein aggregation. This research is modeling and predicting the impact this wide range of biologically relevant solution conditions have on the thermodynamics and kinetics of aggregation and, in the process, dissecting and understanding the roles these various solution factors play. Training objectives include techniques in computational and theoretical modeling, fluorescence and electron microscopy, and enhanced sampling. This research will advance knowledge in general biology, biophysical chemistry, computation biophysics, bioinformatics, and impact areas of biotechnology wherein protein aggregation is undesirable.