Research on the Conformation of Protein Molecules

蛋白质分子构象研究

• 批准号: 9118224
• 负责人: John Fenn
• 金额: $ 10.32万
• 依托单位: Yale University
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1992
• 资助国家: 美国
• 起止时间: 1992-06-15 至 1994-05-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9118224&HistoricalAwards=false
• 关键词: Research; Conformation; Protein; Molecules

Dr. Fenn will use a relatively new technique of Electrospray Mass spectrometry to study the conformation of macromolecules. Specifically, he will: (1) obtain experimental data on the non- covalent forces between amino acid molecules by using tandem mass spectrometry methods to measure the energies required to dissociate small clusters produced by ES ionization; (2) obtain experimental information on the surface area of a protein conformer ion and to investigate the hydrophobic and hydrophilic heterogeneity of that surface. Although emphasis will be placed on proteins in solution, other kinds of polymers will be considered because they may provide useful perspectives. %%% The conformation or "tertiary structure" of protein molecules determines their biological activity and so is a governing factor in many if not most of the chemical processes in living systems. Consequently, it is of vital importance to understand for any protein molecule what its active configuration is along with why and how it comes about. A hoped-for byproduct of these studies will be some insight on mechanisms by which solute ions are formed from charged droplets.

芬恩博士将使用一种相对较新的电喷雾质谱学技术来研究大分子的构象。具体地说，他将：(1)通过使用串联质谱学方法来测量电离产生的小团簇所需的解离能量，从而获得关于氨基酸分子之间非共价力的实验数据；(2)获得关于蛋白质构象离子的表面积的实验信息，并研究该表面的疏水和亲水异质性。虽然重点将放在溶液中的蛋白质上，但也将考虑其他类型的聚合物，因为它们可能提供有用的前景。蛋白质分子的构象或“三级结构”决定了它们的生物活性，因此在生命系统中的许多化学过程中(如果不是大多数的话)也是一个支配因素。因此，对于任何蛋白质分子来说，了解其活性构型是什么，以及它为什么和如何产生是至关重要的。这些研究的一个希望的副产品将是对带电液滴形成溶质离子的机制的一些洞察。