Probing the Energetics of Protein Complex Fragmentation

探索蛋白质复合物断裂的能量学

• 批准号: 7174615
• 负责人: Richard L Beardsley
• 金额: $ 3.21万
• 依托单位: UNIVERSITY OF ARIZONA
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-01-23 至 2007-09-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7174615
• 关键词: Acceleration; Address; Affect; Area; Binding; Biological; Biological Models; Charge; Complex; Crystallography; DNA Sequence Rearrangement; Deposition; Development; Dissociation; Energy Transfer; Environment; Escherichia coli; Freedom; Gases; Goals; Heat shock proteins; Hydrophobic Interactions; Individual; Investigation; Ions; Kinetics; Knowledge; Lead; Learning; Light; Macromolecular Complexes; Methods; Modeling; Multiprotein Complexes; Numbers; Pathway interactions; Pattern; Personal Satisfaction; Phase; Prealbumin; Property; Proteins; Randomized; Range; Research; Role; Structure; Surface; System; Techniques; Testing; Time; Wheat; Work; base; chaperonin; instrument; interfacial; mass spectrometer; monomer; research study; size; trend; voltage

The aim of the proposed research is to characterize the energetics of fragmentation of large multiprotein complexes. Several model systems, including the complexes of small heat shock protein, chaperonin GroEL, and transthyretin, will be studied. The excitation and subsequent dissociation of these systems will be achieved in a modified quadrupole time-of-flight (Q-TOF) mass spectrometer. This instrument allows ion activation by either surface induced dissociation (SID) or collision induced dissociation (CID) and will enable the comparison of these different techniques. The efficient transfer of kinetic to vibrational energy that is achieved via SID will allow the study of multiprotein complexes over a wide range of internal energies. Several factors that likely govern the dissociation of these complexes will be investigated, including activation energy, number and size of subunits in a complex (vibrational degrees of freedom), their interfacial surface area, and types of binding interactions (hydrophobic v. polar). In a broad sense, these studies are aimed to facilitate the development of mass spectrometric strategies for the structural characterization and eventual assignment of biological funtion of multiprotein complexes.

该研究的目的是表征大分子多蛋白质的断裂能量学 配合物几种模型系统，包括小分子热休克蛋白、伴侣蛋白、 GroEL和甲状腺素运载蛋白将被研究。这些系统的激发和随后的解离将 在改进的四极飞行时间（Q-TOF）质谱仪中实现。该仪器允许离子 通过表面诱导解离（SID）或碰撞诱导解离（CID）活化， 这些不同技术的比较。动能到振动能的有效转换， 通过SID实现的将允许在广泛的内能范围内研究多蛋白质复合物。 将研究可能支配这些复合物解离的几个因素，包括 活化能，复合物中亚基的数量和大小（振动自由度），它们的界面 表面积和结合相互作用的类型（疏水性对极性）。从广义上讲，这些研究是 旨在促进结构表征的质谱策略的发展， 最终确定多蛋白复合物的生物学功能。