Protein Interfaces in Solution

溶液中的蛋白质界面

• 批准号: 7540446
• 负责人: Bernard MONTGOMERY PETTITT
• 金额: $ 22.35万
• 依托单位: UNIVERSITY OF HOUSTON
• 依托单位国家: 美国
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-08-01 至 2010-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7540446
• 关键词: Address; Affect; Area; Biochemical; Biological; Biology; Cell model; Cells; Collaborations; Complication; Crowding; Crystallization; Data; Development; Disease; Electrolytes; Entropy; Free Energy; Goals; Hydrophobic Interactions; Hydrophobic Surfaces; Hydrostatic Pressure; Insulin; Investigation; Methods; Modeling; Molecular; Molecular Conformation; Nature; Osmotic Pressure; Planning Theory; Process; Property; Proteins; Psychological Techniques; Research Personnel; Salts; Serratia; Simulate; Solutions; Solvents; Spottings; Structure; Surface; System; Temperature; Testing; Thermodynamics; Water; base; computer studies; dimer; driving force; endonuclease; enthalpy; macromolecule; monomer; physical model; pressure; programs; research study; simulation; small molecule; theories

The primary goal of this proposal is to provide a molecular picture of the basis for the profound effects of cellular crowding and nonideal solution effects in general on biology via the development of new theoretical techniques in conjunction with simulation to provide a molecular picture (theory) of the aspects of the free energy surface that govern protein interfaces and associations in solution. In this project we will produce a molecular picture (theory) of protein interfaces and properties in nonideal solution which are consistent with known and coming thermodynamic and structural data. Test cases including Sm endonuclease and insulin and applications have been chosen to maximize overlap with existing data or collaborations that will yield data of specific relevance to our goal. We will make extensive use of concentration variables in our theoretical and computational studies. Biology rarely uses temperature differences as a mechanism to drive processes; nature more often uses solution composition (concentration of salt, osmolytes, other biomolecules, etc) to affect changes in biological conformation and state of aggregation. We seek to provide a better understanding of these effects.

该提案的主要目标是提供一个分子图景，以了解以下深远影响的基础： 通过新理论的发展，细胞拥挤和非理想溶液对生物学产生总体影响 技术与模拟相结合，提供自由各方面的分子图片（理论） 控制溶液中蛋白质界面和缔合的能量表面。在这个项目中，我们将生产一个 非理想溶液中蛋白质界面和性质的分子图（理论）与 已知和即将到来的热力学和结构数据。测试用例包括 Sm 核酸内切酶和胰岛素 选择应用程序以最大限度地与现有数据或协作重叠，从而产生 与我们的目标具体相关的数据。我们将在我们的研究中广泛使用浓度变量 理论和计算研究。生物学很少使用温差作为驱动机制 流程；大自然更经常使用溶液成分（盐的浓度、渗透剂、其他 生物分子等）影响生物构象和聚集状态的变化。我们力求提供 更好地了解这些影响。