IDBR: TYPE A: Auto-CATM Development: An Instrument for Dynamical Fingerprinting

IDBR：TYPE A：Auto-CATM 开发：动态指纹识别工具

• 批准号: 1556359
• 负责人: Andrea Markelz
• 金额: $ 39.55万
• 依托单位: SUNY at Buffalo
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2016
• 资助国家: 美国
• 起止时间: 2016-04-01 至 2020-03-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1556359&HistoricalAwards=false
• 关键词: IDBR; TYPE; Auto; CATM; Development

An award is made to the State University of New York at Buffalo to develop an instrument to measure the internal vibrations of proteins. Proteins are large molecules with thousands of atoms and perform most cellular functions. Proteins consist of long chains of amino acids, and these chains fold into specific structures. In general, proteins must alter their shape in order to perform their biological function. For example, Hemoglobin, the protein that transports oxygen, changes shape in order for oxygen to bind. The internal vibrations of the protein structure that enable this change in shape are critical for understanding protein function. Recently a method has been devised to measure protein internal vibrations, called crystal anisotropic terahertz microscopy (CATM). The instrumentation and protocol development in this project makes CATM accessible to non-specialists, and enables broad application of the technique. The development of this instrument leads to the interdisciplinary education of two graduate students and two undergraduates. Integrated with the instrument development are educational and outreach activities that include an undergraduate seminar course and a week-long summer program for 7-12th grade inner city students from underrepresented groups. The goal of this project is to produce a compact turn-key spectroscopic system for the routine characterization of intramolecular vibrations of proteins. The technique called crystal anisotropic terahertz (THz) spectroscopy (CATM) uniquely measures these motions. Auto-CATM provides non-experts with the ability to quickly and easily categorize and classify biomacromolecules. The mini-system from Zomega Terahertz Corp. is the starting platform for the final instrument. A proof-of-concept database, and molecular modeling and data visualization software toolbox facilitate the development this new instrument. This instrument provides insights into how intramolecular vibrations are impacted by frequently modified parameters such as binding state and temperature. The technology developed for Auto-CATM also enable new rapid measurements for both bulk and micron scale materials and thus impact solid state physics and materials science.

纽约州立大学布法罗分校获得了开发一种测量蛋白质内部振动的仪器的奖项。蛋白质是具有数千个原子的大分子，执行大多数细胞功能。蛋白质由氨基酸长链组成，这些链折叠成特定的结构。一般来说，蛋白质必须改变其形状才能发挥其生物学功能。例如，血红蛋白（一种运输氧气的蛋白质）会改变形状以便与氧气结合。蛋白质结构的内部振动导致这种形状的变化对于理解蛋白质的功能至关重要。最近设计了一种测量蛋白质内部振动的方法，称为晶体各向异性太赫兹显微镜（CATM）。该项目中的仪器和协议开发使非专业人士也可以使用 CATM，并实现该技术的广泛应用。该仪器的开发导致了两名研究生和两名本科生的跨学科教育。与仪器开发相结合的是教育和外展活动，其中包括本科生研讨会课程和为来自弱势群体的 7 至 12 年级内城学生提供的为期一周的暑期课程。该项目的目标是生产一个紧凑的交钥匙光谱系统，用于蛋白质分子内振动的常规表征。晶体各向异性太赫兹 (THz) 光谱 (CATM) 技术可以独特地测量这些运动。 Auto-CATM为非专家提供了快速、轻松地对生物大分子进行分类和分类的能力。 Zomega Terahertz Corp. 的迷你系统是最终仪器的起始平台。概念验证数据库、分子建模和数据可视化软件工具箱促进了这种新仪器的开发。该仪器可深入了解经常修改的参数（例如结合状态和温度）如何影响分子内振动。为 Auto-CATM 开发的技术还可以对块状和微米级材料进行新的快速测量，从而影响固态物理学和材料科学。

项目成果

The 2017 terahertz science and technology roadmap

2017年太赫兹科技路线图

• DOI: 10.1088/1361-6463/50/4/043001
• 发表时间: 2017-02
• 期刊: Journal of Physics D: Applied Physics
• 作者: Dhillon, S S;Vitiello, M S;Linfield, E H;Davies, A G;Hoffmann, Matthias C;Booske, John;Paoloni, Claudio;Gensch, M;Weightman, P;Williams, G P;et al
• 通讯作者: et al

Modulated orientation-sensitive terahertz spectroscopy

调制定向敏感太赫兹光谱

• DOI: 10.1364/prj.4.0000a1
• 发表时间: 2016-06
• 期刊: Photonics Research
• 影响因子: 7.6
• 作者: Singh, Rohit;George, Deepu Koshy;Bae, Chejin;Niessen, K. A.;Markelz, A. G.
• 通讯作者: Markelz, A. G.

Moving in the Right Direction: Protein Vibrational Steering Function

朝着正确的方向前进：蛋白质振动引导功能

• DOI: 10.1016/j.bpj.2016.12.049
• 发表时间: 2017-03
• 期刊: Biophysical Journal
• 影响因子: 3.4
• 作者: Niessen, Katherine A.;Xu, Mengyang;Paciaroni, Alessandro;Orecchini, Andrea;Snell, Edward H.;Markelz, Andrea G.
• 通讯作者: Markelz, Andrea G.