DIRECT MEASUREMENT OF FORCES BETWEEN MEMBRANES OR MACROMOLECULES

直接测量膜或大分子之间的力

• 批准号: 3838552
• 负责人: V A PARSEGIAN
• 金额: --
• 依托单位: CENTER FOR INFORMATION TECHNOLOGY
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3838552
• 关键词: chemical hydration; collagen; intermolecular interaction; lipid bilayer membrane; macromolecule; measurement; membrane activity; molecular biology; protein biosynthesis; quaternary ammonium compound; temperature

The ability to measure directly the forces between membranes or between macromolecules is creating a new logic for thinking about molecular recognition, assembly, and folding. The outstanding feature of interaction is that as molecules or membranes approach contact, the important work of approach involves removal of organized water solvent from the apposing surfaces. These "hydration forces" are now recognized to act in materials as diverse as lipid bilayers, proteins, DNA double helices, and stiff polysaccharides. During the current year a first direct measurement of forces between protein molecules (type I collagen triple helices) has succeeded. It has been shown that the force has all the features characteristic of hydration forces. The temperature dependence of the force is similar to that observed in ordered arrays of DNA molecules. This shows that physical nature of temperature-favored assembly in DNA and proteins might be similar. Temperature-favored assembly is a common feature of many biologically important processes. The theory of temperature-favored assembly induced by attractive hydration forces between hydrophilic molecules has been developed. Measurement of interaction forces between dihexadecyldimethylammonium acetate bilayers has demonstrated that neither thermal-mechanical undulations nor molecular protrusions contribute significantly to hydration forces between lipid bilayers.

能够直接测量膜之间的力或 大分子之间正在创造一种新的思考逻辑 分子识别、组装和折叠。 突出特点 相互作用的关键在于，当分子或膜接近接触时， 该方法的重要工作涉及去除有组织的水溶剂 从相对的表面。 这些“水合力”现在 公认可在脂质双层、蛋白质、DNA 等多种材料中发挥作用 双螺旋和刚性多糖。 在本年度内 首次直接测量蛋白质分子之间的力（I 型 胶原蛋白三螺旋）已成功。 已经表明， 力具有水合力的所有特征。 这 力的温度依赖性类似于在 DNA 分子的有序阵列。 这表明物理性质 DNA 和蛋白质中有利于温度的组装可能是相似的。 有利于温度的组装是许多生物学的共同特征 重要流程。 有利温度组装理论 由亲水分子之间的吸引力水合力引起 已经开发出来了。 测量之间的相互作用力 二十六烷基二甲基乙酸铵双层已证明 既没有热机械波动也没有分子突起 对脂质双层之间的水合力有显着贡献。