Protein Interfaces in Solution

溶液中的蛋白质界面

• 批准号: 7742644
• 负责人: Bernard MONTGOMERY PETTITT
• 金额: $ 22.13万
• 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 2011-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7742644
• 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.

该提案的主要目的是提供分子图的基础，以实现深远影响 通过开发新理论，总体上对生物学的细胞拥挤和非理想解决方案影响 与模拟结合使用的技术提供了自由方面的分子图片（理论） 控制蛋白质界面和溶液中关联的能量表面。在这个项目中，我们将产生一个 非理想溶液中蛋白质界面和特性​​的分子图片（理论）与与 已知和即将到来的热力学和结构数据。测试用例包括SM内切核酸酶和胰岛素 并选择了应用程序来最大程度地与现有数据或将产生的合作重叠 与我们目标的特定相关性数据。我们将大量使用浓度变量 理论和计算研究。生物学很少使用温度差为驱动机制 过程；自然更多地使用溶液组成（盐的浓度，渗透液，其他 生物分子等）影响生物构象和聚集状态的变化。我们试图提供 更好地理解这些影响。