STUDYING TRPZIPS USING RESONANCE RAMAN SPECTROSCOPY

使用共振拉曼光谱研究 TRPZIPS

• 批准号: 7598455
• 负责人: THOMAS G. SPIRO
• 金额: $ 0.08万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-09-01 至 2008-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7598455
• 关键词: Amides; Area; Circular Dichroism Spectroscopy; Computer Retrieval of Information on Scientific Projects Database; Funding; Grant; Institution; Kinetics; Lasers; Measurement; Methods; Monitor; Motion; Object Attachment; Proteins; Raman Spectrum Analysis; Research; Research Personnel; Resources; Series; Site; Source; System; Time; Tryptophan; United States National Institutes of Health; infrared spectroscopy; protein aminoacid sequence; temperature jump

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. Folding dynamics of beta-hairpins has been a prominent area of studies in the Gai group. We have investigated the structural stability and folding kinetics of a series of beta-hairpins, namely: tryptophan zippers, by static Infrared spectroscopy, Circular Dichroism and the Infrared temperature jump method. To further extend our understanding of this system, we plan to collaborate with Dr. Spiros lab and use Resonance Raman Spectroscopy in a time resolved mode to study the dynamics of motion of tryptophan zippers (Trpzips). Tryptophan is an aromatic residue and is believed to be involved in H- bonding interactions, and thus can be used as probes of motion at various sites in the protein. Therefore, Trpzips are an ideal system for Resonance Raman Spectroscopy because we can use wavelength-selective laser excitation to monitor Resonance Raman spectra of the tryptophan sidechains and thus monitor the motion of Trpzips. We plan look at investigate Trptophan residues in the Trpzips at 229 nm wavelength and amide bands excited below 200 nm wavelength. The sequence of the peptide used in the current study is as following: Trpzip2: SWTWENGKWTWK. For preliminary studies, we would like to do one set of static measurement and 1 to 5 sets of T-jump measurements so as to check the activation energy. If we obtain favorable results we will extend the study further.

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， 因此可以在其他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。 折叠动力学的β-发夹一直是一个突出领域的研究在盖组。我们研究了一系列的β-发夹，即：色氨酸拉链，静态红外光谱，圆二色性和红外温度跳跃方法的结构稳定性和折叠动力学。为了进一步扩展我们对这个系统的理解，我们计划与斯皮罗博士合作。的实验室，并使用共振拉曼光谱在时间分辨模式，以研究色氨酸拉链（Trpzips）的运动动力学。色氨酸是芳香族残基，并且被认为参与氢键相互作用，因此可以用作蛋白质中各个位点的运动探针。因此，Trpzips是共振拉曼光谱的理想系统，因为我们可以使用波长选择性激光激发来监测色氨酸侧链的共振拉曼光谱，从而监测Trpzips的运动。我们计划在229 nm波长下研究Trpzips中的色氨酸残基，并在200 nm波长以下激发酰胺带。本研究中使用的肽的序列如下：Trpzip 2：SWTWENGKWTWK。为了初步研究，我们想做一组静态测量和1至5组T-跳跃测量，以检查活化能。如果我们获得有利的结果，我们将进一步扩大研究。