Probing the Energetics of Protein Complex Fragmentation

探索蛋白质复合物断裂的能量学

• 批准号: 6997978
• 负责人: Richard L Beardsley
• 金额: $ 4.21万
• 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 2008-01-22
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6997978
• 关键词: bioenergetics; biotechnology; chemical association; heat shock proteins; mass spectrometry; molecular chaperones; postdoctoral investigator; protein protein interaction; protein structure function; proteomics; retinoid binding proteins; thyroid hormone binding protein

DESCRIPTION (provided by applicant): 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.

描述（由申请人提供）： 拟议的研究的目的是表征大的多蛋白质复合物的碎片的能量学。几个模型系统，包括复合物的小热休克蛋白，伴侣GroEL，和甲状腺素运载蛋白，将进行研究。这些系统的激发和随后的解离将在改进的四极杆飞行时间（Q-TOF）质谱仪中实现。该仪器允许通过表面诱导解离（SID）或碰撞诱导解离（CID）进行离子活化，并将能够比较这些不同的技术。通过SID实现的动能到振动能的有效转移将允许在广泛的内能范围内研究多蛋白质复合物。几个因素，可能支配这些复合物的解离将被调查，包括活化能，数量和大小的亚基在一个复杂的（振动自由度），它们的界面表面积，和类型的结合相互作用（疏水性与极性）。从广义上讲，这些研究旨在促进质谱策略的发展，用于多蛋白复合物的结构表征和最终的生物学功能分配。