International Collaboration in Chemistry: Electron Delocalization in Polypeptide Structure and Stability

国际化学合作：多肽结构和稳定性中的电子离域

• 批准号: 1124944
• 负责人: Ronald Raines
• 金额: $ 36万
• 依托单位: University of Wisconsin-Madison
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-10-01 至 2014-09-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1124944&HistoricalAwards=false
• 关键词: International; Collaboration; Chemistry; Electron; Delocalization

With this International Collaboration in Chemistry (ICC) award, the Chemistry of Life Processes (CLP) program of the Division of Chemistry is supporting collaborative work by Professor Ronald T. Raines of the University of Wisconsin-Madison and Professor Derek N. Woolfson of the University of Bristol, to carry out fundamental studies on protein structure and stability, with an eye toward understanding secondary orbital interactions. Research in the Woolfson laboratory in the UK is supported by the partnering agency, the Engineering and Physical Sciences Research Council (EPSRC). This award is being co-funded by the NSF Office of International Science and Engineering (OISE).Protein structures and assemblies are directed, stabilized, and governed by a wide variety of non-covalent interactions. Recently, work from this collaborative team suggested that a lesser-known force, based upon n-to-pi* interactions, is widespread in protein structures, and likely plays roles in stability and function. Building on this new finding, the proposed research has two overarching objectives: (1) using bioinformatics to probe n-to-pi* and analogous interactions in high-resolution polypeptide structures of the available public databases, namely the Cambridge Structural Database (CSD) and the RCSB (Brookhaven) Protein Data Bank (PDB); and (2) using chemistry to explore the possibility of stabilizing peptide and protein structures by enhancing n-to-pi* interactions through backbone chemical modification. Outcomes could include a better understanding of non-covalent forces in peptide and protein structures, and a general means to stabilize those structures.In addition to scientific broader impacts in potentially changing the way chemists think about conformation and orbital interactions in peptides, there are significant educational broader impacts. This NSF-EPSRC ICC award will enable participating students and postdoctorates to experience international collaborative research first hand with colleagues in the partnering laboratory.

通过这一国际化学合作（ICC）奖，化学过程的化学过程（CLP）计划支持威斯康星大学麦迪逊分校的罗纳德·T·雷恩斯教授的合作工作，布里斯托尔大学的德里克·伍尔夫森（Derek N. 在英国伍尔夫森实验室的研究得到了合作伙伴机构，工程和物理研究委员会（EPSRC）的支持。 该奖项由NSF国际科学与工程办公室（OISE）共同资助。蛋白质结构和集会由多种非共价互动指导，稳定和统治。 最近，该协作团队的工作表明，基于N到Pi*相互作用的鲜为人知的力量在蛋白质结构中广泛存在，并且可能在稳定性和功能中起着作用。 在这一新发现的基础上，拟议的研究具有两个总体目标：（1）使用生物信息学来探测可用公共数据库的高分辨率多肽结构中的n-to-pi*和类似的相互作用，即剑桥结构数据库（CSD）和RCSB（Brookhaven）Protein Data Bank（pddb）（pddb）（pddb）; （2）使用化学通过通过骨架化学修饰来增强N到Pi*相互作用来探索稳定肽和蛋白质结构的可能性。结果可能包括更好地理解肽和蛋白质结构中的非共价力，以及稳定这些结构的一般手段。除了科学的广泛影响外，还可以改变化学家对肽中的构象和轨道相互作用的看法，具有重大的受教育程度。 NSF-EPSRC ICC奖将使参与的学生和博士后与合作实验室的同事第一手进行国际合作研究。