PRESSURE-INDUCED PROTEIN GLASS TRANSITION AND WATER-PROTEIN INTERACT

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 当温度变化时，蛋白质会经历“玻璃化转变”，这是蛋白质动力学中的一种转变。这种蛋白质玻璃化转变与蛋白质功能高度相关。当温度低于玻璃化转变点时，蛋白质分子就不再发挥其生物功能。因此，研究蛋白质玻璃化转变可能有助于深入了解蛋白质动力学与功能之间的关系。推测蛋白质分子周围的水在诱导蛋白质玻璃化转变中起着重要作用。然而，具体的机制仍是一个悬而未决的问题。最近，研究人员提出了一种可能的机制，涉及水的相变，高密度液体(HDL)和低密度液体(LDL)的水转变。鉴于高密度脂蛋白和低密度脂蛋白水的存在存在争议，这一拟议的机制需要更多的实验审查。在我们的研究中，我们建议利用高压蛋白质结晶学技术和同步辐射来研究蛋白质的玻璃化转变。在国际象棋上测量结构时，将对牛胰腺核糖核酸酶A的蛋白质晶体施加不同的压力水平。结晶学结果将提供蛋白质和周围水随压力变化的静态结构和动力学。蛋白质玻璃化转变和水动力学以及它们的结构对压力的依赖关系可能提供关于水、蛋白质动力学、蛋白质结构和蛋白质功能之间相互作用的宝贵信息。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Proteins undergo the `glass transition`, a transition in protein dynamics, when subjected to temperature variation. This protein glass transition is highly correlated with protein function. A protein molecule ceases to perform its biological function at temperatures below the glass transition points. Therefore, studying the protein glass transition may provide insight to the correlation between protein dynamics and function. It is speculated that the water surrounding a protein molecule plays an important role in inducing protein glass transition. However, the exact mechanism is still an open question. Recently, researchers proposed a probable mechanism involving the phase transition of water, high density liquid (HDL) and low density liquid (LDL) water transition. Given the controversy over the existence of HDL and LDL water, this proposed mechanism demands more experimental scrutiny. In our study, we propose to utilize the high pressure protein crystallography technique and synchrotron radiation to study the protein glass transition. Varying pressure levels will be applied to protein crystals of bovine pancreatic ribonuclease A while the structure is measured at CHESS. The crystallography results will provide both the static structure and dynamics of the protein and surrounding water versus pressure. The dependence of the protein glass transition and water dynamics as well as their structure upon pressure may provide precious information about the interplay among water, protein dynamics, protein structure and protein function.