2D IR OF GUANIDINE IN WATER

水中胍的二维红外图

• 批准号: 8362573
• 负责人: Jane Marie Vanderkooi
• 金额: $ 1.95万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-06-01 至 2012-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362573
• 关键词: Binding; Biology; Coupling; Frequencies; Funding; Goals; Grant; Guanidines; Hydrogen Bonding; Investigation; Ions; Laboratories; Microscopic; National Center for Research Resources; Optics; Principal Investigator; Process; Proteins; Research; Research Infrastructure; Resources; Solutions; Source; Spectroscopy, Fourier Transform Infrared; Stretching; Structure; United States National Institutes of Health; Water; cost; physical property

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Recent FTIR investigations of the OH stretch mode of water in guanidine solutions revealed a large frequency shift to lower frequency of the O-H stretch mode after guanidine addition, arising questions about the structure of the solvation shell of water molecules around the guanidine ions. Guanidine is often used as a protein denaturant. It may act as a denaturant because it binds to proteins directly since it has 3 NH2 groups that mimic water molecules in their H-bonding ability. The goal of this project is to generate a microscopic description of the interaction between guanidine and water and deduce why guanidine is so effective as a denaturant in biology. It has been postulated that guanidine changes the structure of the water network. By using dual frequency 2D-IR, we are able to visualize the interaction between guanidine and the surrounding water as well as the water-water interactions. By using 2D-IR, we should be able to tell between the following: Are the water molecules surrounding guanidine isolated from the bulk water? Do the frequency fluctuations of the OH stretch modes of the solvation shell manifest coupling to the ion? Or are the water molecules surrounding guanidine similar in their physical properties to the bulk water?

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 最近对鸟选择素溶液中的OH伸展水模式的FTIR研究表明，添加鸟选择后向O-H伸展模式的较低频率转移，引起了有关鸟嘌呤离子周围水分子溶剂壳的结构的问题。鸟嘌呤通常用作蛋白质变性剂。它可以用作变性剂，因为它直接与蛋白质结合，因为它具有3个NH2基团，它们模仿水分子的H键能力。 该项目的目的是生成对鸟选择和水之间相互作用的显微镜​​描述，并推断为什么鸟选择素在生物学上如此有效。据推测，鸟选择改变了水网络的结构。通过使用双频率2D-IR，我们能够可视化鸟选择和周围水以及水水相互作用之间的相互作用。通过使用2D-IR，我们应该能够在以下方面分辨：是否从大量水中分离出鸟苷的水分子？溶剂壳的OH拉伸模式的频率波动是否表现为离子？还是鸟嘌呤周围的水分子在物理特性上与大量水相似？