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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 β发pins的折叠动力学一直是GAI组的重要研究领域。我们已经通过静态红外光谱，圆形二色性和红外温度跳跃方法研究了一系列β发pins的结构稳定性和折叠动力学。为了进一步扩展我们对该系统的理解，我们计划与Spiro博士的实验室合作，并在时间解析模式下使用共振拉曼光谱来研究色氨酸拉链运动的运动动力学（TRPZIPS）。色氨酸是一种芳族残基，被认为与H键相互作用有关，因此可以用作蛋白质中各个位点的运动探针。因此，TRPZIP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Sidechains的共振拉曼光谱，从而监测TRPZIPS的运动。我们计划查看在229 nm波长的TRPZIP中研究Trptophan残基，并在200 nm波长以下激发的酰胺带。当前研究中使用的肽的序列如下：TRPZIP2：SWTWENGKWTWK。对于初步研究，我们想进行一组静态测量和1至5组T-JUMP测量，以检查激活能量。如果我们获得有利的结果，我们将进一步扩展研究。