HIGH PRESSURE EFFECTS ON PROTEIN CONFORMATION & DYNAMICS

酰胺质子交换速率的压力依赖性 在葡萄球菌核酸酶H124 L中的作用。 动力学 溶剂和蛋白质之间的氢交换是一个强有力的探针 蛋白质在溶液中的结构，动力学和稳定性， 因为即使在这样的条件下， 比变性状态更稳定，除了少数核心上的氢， 肽氮将与水交换。 在解释 动力学，Linderstrom-Lang模型的NH-交换，和 假设EX 2交换机制。 开盘率确定 (the从“封闭”到“开放”的构象变化速率 交换被认为发生的国家）在一些 不同的压力，并通过计算的依赖性 在压力上处于打开和关闭状态之间的平衡位置， 可以确定两者之间的偏摩尔体积的变化 states.

The pressure dependence of the exchange rate of the amide protons in staphylococcal nuclease H124L is being investigated. The kinetics of hydrogen exchange between solvent and protein are a powerful probe of the structure, dynamics and stability of proteins in solution, since even under conditions such that the native state is much more stable than the denatured state, the hydrogens on all but a few core peptide nitrogens will exchange with water. In interpreting the kinetics, the Linderstrom-Lang model of NH-exchange is applied, and an EX2 exchange mechanism is assumed. The opening rate is determined (the rate of conformational change from the "closed" to the "open" state from which the exchange is thought to take place) at a number of different pressures, and by calculating the dependence of the equilibrium position between the open and closed states on pressure, one can determine the change in partial molar volumes between the two states.