PRESSURE DISSOCIATION OF OLIGOMERIC PROTEINS AND VIRUSES

寡聚蛋白和病毒的压力解离

• 批准号: 2168540
• 负责人: GREGORIO WEBER
• 金额: $ 9.27万
• 依托单位: UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN
• 依托单位国家: 美国
• 财政年份: 1978
• 资助国家: 美国
• 起止时间: 1978-05-01 至 1997-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2168540
• 关键词: actins; biophysics; chemical aggregate; chemical condensation; chemical kinetics; chemical stability; conformation; fluorescence polarization; fluorescence spectrometry; globular protein; hydrostatic pressure; molecular dynamics; myosins; protein denaturation; protein folding; stop flow technique; temperature; thermodynamics

This revised application contains a research proposal to address two clearly defined and related problems: 1. The denaturation of single peptide chain proteins by hydrostatic pressure at temperatures below 0 degrees C, a possibility that depends on the decrease of the melting point of water to -20 degrees C at 2 kbar. 2. The effects of hydrostatic pressure upon myosin, actin and their mixed aggregates, at various temperatures. From these observations we shall derive the respective thermodynamic parameters for the transitions of peptide chains from globular to unfolded states, and those that correspond to states of actin and myosin aggregates believed to be of importance in motility. The results will be interpreted according to a recent theory of the author which relates the thermodynamic parameters to the differences in the average bond strengths of the reactants and products, and derives from these the characteristic pressure-temperature-volume relations of the system.

此修订后的应用程序包含一个研究建议，以解决两个 明确定义和相关问题：1。单一的变性 在低于0 ℃的温度下用静水压力测定肽链蛋白质 摄氏度，这种可能性取决于熔化的减少。 在2千巴下，将水的温度降至-20摄氏度。 2.流体静力学的影响 在不同的压力下，肌球蛋白，肌动蛋白及其混合聚集体， 温度 从这些观察，我们将得出相应的热力学 肽链从球形到球形的转变参数 未折叠状态，以及与肌动蛋白和肌球蛋白状态相对应的状态 聚集体被认为在运动中具有重要性。 结果将 根据作者最近的一个理论来解释， 热力学参数对平均键差的影响 反应物和产物的强度，并从这些 系统的特征压力-温度-体积关系。