Non-covalent Complexes

该奖项是根据2009年《美国复苏和再投资法案》(公法111-5)提供资金的。在这个由化学系实验物理化学项目资助的奖项中，加州大学圣巴巴拉分校的迈克尔·鲍尔斯教授探索了为什么生命系统中的肽和蛋白质都是由L氨基酸组成的问题，氨基酸是生物学中最深的谜团之一。鲍尔斯教授和他的学生将从几个简单的多肽模型系统开始，这些系统有多种手性混合形式可用。这些多肽足够小(5或6个氨基酸长)，因此可以对它们进行良好的理论研究，以帮助理解观察到的折叠和聚集趋势随其手性纯度的变化。这些多肽家族还将为该提案的第二个主要推动力--淀粉样蛋白形成机制提供一个入口。淀粉样蛋白在复杂的生命系统中普遍存在，并与许多严重疾病(阿尔茨海默氏症、2型糖尿病等)有关。我们的目标是了解聚集过程，以及最初卷曲的或α-螺旋低聚体系如何最终成为大的β-折叠组件。作为这一努力的一部分，鲍尔教授的团队将与柏林弗里茨·哈伯研究所的格哈德·梅杰和格特·冯·赫尔登展开合作。该小组正在为这项工作建造一台符合鲍尔教授规格的最先进的仪器，以配合该设施正在建设的新的自由电子激光器。最后，研究人员开始研究与2型糖尿病有关的一个具有重要生物学意义的淀粉样蛋白系统，即37个残基的IAPP或胰淀素多肽。人类野生型多肽迅速形成大的寡聚体，但许多非常相似的多肽却不能。初步数据表明，致密的集合体会导致纤维形成(从而导致疾病)，而相同数量的寡聚体的细长集合体不会进一步聚集。为了充分理解这些初步结果，我们计划进行建模和进一步的实验。美国的科学教育持续低迷，威胁到我们在创新和技术发展方面的世界领先地位。问题很早就开始了。五年级被认为是儿童科学发展的第一个“去”或“不去”的指标。在UCSB，有一个强大的五年级外展计划，由一名前小组成员发起和维持，并得到现任研究小组成员的持续帮助。鲍尔斯教授决定解决年轻人的第二个“去”或“不去”的决定时间--他们的高中时代。他的团队正在制定一个推广计划，让所有团队成员向高中班级展示他们的研究项目，并讲述他们个人的科学故事，以及他们是如何进入UCSB研究生院的。对其中一名小组成员进行了初步试验，结果令人鼓舞。随着项目的发展，更多的UCSB教员和研究小组将被纳入其中。

This award is funded under the American Recovery and Reinvestment Act of 2009 (Public Law 111-5). In this award funded by the Experimental Physical Chemistry Program of the Division of Chemistry, Professor Michael Bowers of University of California, Santa Barbara, explores the question of why peptides and proteins in living systems are soley composed of L-amino acids - one of the deepest mysteries in biology. Professor Bowers and his students will start with several simple model systems of peptides that are available in a wide range of chirally mixed forms. These peptides are small enough (5 or 6 amino acids long) that good theory can be done on them to help understand observed changes in their folding and aggregation tendencies as a function of their chiral purity. These peptide families will also provide an entrée into a second major thrust of the proposal - amyloid formation mechanisms. Amyloids are ubiquitous in complex living systems and are implicated in many serious diseases (Alzheimer's, type 2 diabetes, etc.). The goal is to understand the aggregation process and how initially coiled or alpha-helical oligomeric systems end up as large beta-sheet assemblies. As part of this effort Professor Bower's team will initiate a collaboration with Gerhard Meijer and Gert Von Helden at the Fritz Haber Institute in Berlin. This group is building a state of the art instrument to Professor Bower's specifications for this work to couple with a new free electron laser under construction at that facility. Finally the researchers have initiated studies on a related biologically important amyloid system, the 37 residue IAPP or amylin peptide, involved in type 2 diabetes. The human wild type peptide rapidly forms large oligomers but a number of very similar peptides do not. Preliminary data implicate compact assemblies as leading to fibril formation (and hence disease) while elongated assemblies of the same oligomer number do not aggregate further. Modeling and further experiments are planned to fully understand these initial results. Science education in the United States is in a sustained downturn that threatens our world leadership in both innovation and technology development. The problems start early. The 5th grade has been targeted as the first "go" or "no go" indicator in a child's scientific development. At UCSB there is a strong outreach program at the 5th grade level initiated and sustained by a former group member with continuing help from current research group members. Professor Bowers decided to tackle the second "go" or "no go" decision time in young adults - their high school years. His group is developing an outreach program using all group members to present their research projects to high school classes and to relate their personal scientific stories and how they ended up in graduate school at UCSB. A preliminary trial with one of the group members has been run with encouraging results. Additional UCSB faculty and research groups will be incorporated as the program grows.