PRESSURE DISSOCIATION OF OLIGOMERIC PROTEINS AND VIRUSES

这份修订后的申请包含一项研究提案，旨在解决两个问题 明确定义及相关问题：1.单细胞变性 温度低于0℃的静水压下的多肽链蛋白质 摄氏度，这一可能性取决于融化的减少 在2千巴时，水点降至零下20摄氏度。2.静水压力的影响 肌球蛋白、肌动蛋白及其混合聚集体在不同条件下的压力 温度。 从这些观测中，我们将得出各自的热力学 多肽链从球状到球状转变的参数 展开状态，以及与肌动蛋白和肌球蛋白状态相对应的状态 被认为对运动性有重要影响的聚集体。结果将会是 根据作者最近的一种理论进行解释，该理论涉及 热力学参数对平均键差异的影响 反应物和产物的强度，并由此得出 系统的压力-温度-体积特征关系。

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.