Protein Structure, Dynamics, and Folding via Ultrafast Multidimensional Infrared Spectroscopy

通过超快多维红外光谱研究蛋白质结构、动力学和折叠

• 批准号: 1310693
• 负责人: Nien-Hui Ge
• 金额: $ 45万
• 依托单位: University of California-Irvine
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2013
• 资助国家: 美国
• 起止时间: 2013-07-01 至 2017-06-30
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1310693&HistoricalAwards=false
• 关键词: Protein; Structure; Dynamics; Folding; via

In this award the Chemistry of Life Processes Program supports Professor Nien-Hui Ge of the University of California at Irvine to use femtosecond multidimensional infrared (MultiD IR) spectroscopy to study the conformational dynamics, distributions, and folding of peptides. The goal is to provide detailed knowledge of protein structure and dynamics that is essential to the understanding of biological processes. The proposed work includes investigating the interplay between helical and extended structures, determining conformational distributions of nonfolding peptides, and elucidating protein-membrane interactions. MultiD IR experiments access the backbone and side chain vibrational modes of peptides, and provide data that reveal the angles, distances, and correlations between structural units. Isotope editing and incorporating IR probes at selected locations enhance the spatial resolution, facilitate the assignment of resonances, and extend the method to larger peptides and tertiary contacts. The effects of temperature, pH, solvent, and chain length are investigated to understand the factors that control protein stability. Proteins, long chains of peptides, fold rapidly into complex shapes that affect their function and how they bind with other molecules. Detailed knowledge of peptides and larger proteins - structure, dynamics, and folding can shed light on protein misfolding that characterizes many diseases. Understanding how proteins interact with membranes also informs the design of novel functional molecules, potentially useful for medicine. MultiD IR spectroscopy is a laser technique that can determine the shape and behavior of a peptide by studying the infrared light emitted after it was "photographed" using laser pulses at a "shutter speed" faster than one trillionth of a second. Graduate students and postdoctoral researchers participating in the research gain valuable experience with advanced laser techniques and core physical sciences that can strengthen their future career development. This project is also integrated with outreach efforts on maintaining an online spectrum database and contributing lectures and laboratory courses for K-12 students.

在该奖项中，生命过程化学项目支持加州大学欧文分校的葛念辉教授使用飞秒多维红外(MultiD IR)光谱研究多肽的构象动力学、分布和折叠。目标是提供对理解生物过程至关重要的蛋白质结构和动力学的详细知识。拟议的工作包括研究螺旋结构和延伸结构之间的相互作用，确定非折叠多肽的构象分布，以及阐明蛋白质-膜相互作用。多维红外实验获得了多肽的主链和侧链振动模式，并提供了揭示结构单元之间的角度、距离和相关性的数据。同位素编辑和在选定位置加入红外探测器提高了空间分辨率，促进了共振的分配，并将该方法扩展到更大的多肽和三级接触。考察了温度、pH、溶剂和链长对蛋白质稳定性的影响，以了解控制蛋白质稳定性的因素。蛋白质是多肽的长链，它会迅速折叠成复杂的形状，影响它们的功能以及它们与其他分子的结合方式。对多肽和更大的蛋白质--结构、动力学和折叠--的详细了解可以帮助我们了解蛋白质错误折叠，这种错误折叠是许多疾病的特征。了解蛋白质如何与膜相互作用也有助于设计新的功能分子，这可能对医学有用。多维红外光谱是一种激光技术，它可以通过研究多肽被以快于万亿分之一秒的“快门速度”的激光脉冲“拍摄”后发射的红外光来确定其形状和行为。参与研究的研究生和博士后研究人员在先进的激光技术和核心物理科学方面获得了宝贵的经验，可以加强他们未来的职业发展。该项目还与维护在线频谱数据库和为K-12学生提供讲座和实验室课程的外联工作相结合。

项目成果

Ultrafast vibrational dynamics of the tyrosine ring mode and its application to enkephalin insertion into phospholipid membranes as probed by two-dimensional infrared spectroscopy

二维红外光谱探测酪氨酸环模式的超快振动动力学及其在脑啡肽插入磷脂膜中的应用

• DOI: 10.1063/5.0054428
• 发表时间: 2021
• 期刊: The Journal of Chemical Physics
• 作者: Vinogradov, Ilya;Feng, Yuan;Kumar, S. K. Karthick;Guo, Chenxu;Udagawa, Nina Saki;Ge, Nien-Hui
• 通讯作者: Ge, Nien-Hui

Wavelength and Polarization Dependence of Second-Harmonic Responses from Gold Nanocrescent Arrays

金纳米月牙阵列二次谐波响应的波长和偏振依赖性

• DOI: 10.1021/acs.jpcc.0c05548
• 发表时间: 2020
• 期刊: The Journal of Physical Chemistry C
• 作者: Maekawa, Hiroaki;Drobnyh, Elena;Lancaster, Cady A.;Large, Nicolas;Schatz, George C.;Shumaker-Parry, Jennifer S.;Sukharev, Maxim;Ge, Nien-Hui
• 通讯作者: Ge, Nien-Hui