PRESSURE-INDUCED PROTEIN GLASS TRANSITION AND WATER-PROTEIN INTERACT

压力诱导的蛋白质玻璃化转变和水-蛋白质相互作用

• 批准号: 7955589
• 负责人: SOL M GRUNER
• 金额: $ 5.49万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-07-01 至 2010-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955589
• 关键词: Biological Process; Cattle; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Dependence; Funding; Glass; Grant; Institution; Liquid substance; Measures; Pancreatic ribonuclease; Phase Transition; Play; Protein Dynamics; Proteins; Research; Research Personnel; Resources; Role; Source; Structure; Techniques; Temperature; United States National Institutes of Health; Variant; Water; density; insight; pressure; protein function; protein structure; synchrotron radiation

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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 当受到温度变化时，蛋白质经历“玻璃化转变”，即蛋白质动力学的转变。这种蛋白质玻璃化转变与蛋白质功能高度相关。蛋白质分子在低于玻璃化转变点的温度下停止执行其生物功能。因此，研究蛋白质的玻璃化转变可以提供洞察蛋白质动力学和功能之间的相关性。据推测，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，确切的机制仍然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）水的转变。鉴于对高密度脂蛋白和低密度脂蛋白水的存在争议，这种拟议的机制需要更多的实验审查。在本研究中，我们提出利用高压蛋白质晶体学技术和同步辐射来研究蛋白质的玻璃化转变。在CHESS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。晶体学结果将提供蛋白质和周围水与压力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性可以提供关于水、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。