DYNAMICS OF PROTEIN RNASE A & WATER-PROTEIN INTERACT AT DIFFERENT TEMPERATURES

蛋白质 RNA 酶 A 的动力学

• 批准号: 7721339
• 负责人: SOL M GRUNER
• 金额: $ 3.27万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-08-01 至 2009-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721339
• 关键词: Behavior; Computer Retrieval of Information on Scientific Projects Database; Data Set; Endoribonucleases; Environment; Exhibits; Funding; Glass; Grant; Hydration status; Institution; Mothers; Pancreatic ribonuclease; Property; Protein Dynamics; Proteins; Range; Research; Research Personnel; Resources; Ribonucleases; Solvents; Source; Structure; Temperature; United States National Institutes of Health; Variant; Water; distilled alcoholic beverage; pressure; research study

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 are known to undergo `glass transition` when subjected to temperature variations at ambient pressure. This transition involves dynamics of protein molecules and their enzymatic activity. From crystallographic Debye-Waller factors and protein crystal structures, the relation between protein dynamics and enzymatic activity was established. Though it is widely accepted that protein glass transition is highly related to the hydration water, the exact mechanisms are still lacking. Therefore, our aim is to understand these exact mechanisms and the interactions between water and protein molecules. In the first step of the study, we will grow two kinds of RNase A crystals from two different mother liquors which impose two different solvent environments to protein molecules. The complete dataset for these crystals will be collected at 9 temperature points ranging from 98 K to 320 K (one complete dataset for each point). These two kinds of crystals are expected to exhibit different glass transition behaviors due to different solvent environments, which will confirm the proposed relation between protein dynamics and water properties. The previous experiments showed our RNase A crystals have good diffraction quality.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 中心，不一定是研究者的机构。 已知蛋白质在环境压力下受到温度变化时会经历“玻璃化转变”。这种转变涉及蛋白质分子的动力学及其酶活性。根据晶体学德拜-沃勒因子和蛋白质晶体结构，建立了蛋白质动力学和酶活性之间的关系。尽管人们普遍认为蛋白质玻璃化转变与水合水高度相关，但仍缺乏确切的机制。因此，我们的目标是了解这些确切的机制以及水和蛋白质分子之间的相互作用。在研究的第一步中，我们将从两种不同的母液中生长两种 RNase A 晶体，这两种母液对蛋白质分子施加两种不同的溶剂环境。这些晶体的完整数据集将在 98 K 至 320 K 的 9 个温度点收集（每个点一个完整的数据集）。由于不同的溶剂环境，这两种晶体预计会表现出不同的玻璃化转变行为，这将证实蛋白质动力学和水性质之间的关系。之前的实验表明我们的 RNase A 晶体具有良好的衍射质量。