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MRI: Acquisition of a circular dichroism spectropolarimeter for research and training of undergraduates at Gettysburg College

MRI: Acquisition of a circular dichroism spectropolarimeter for research and training of undergraduates at Gettysburg College
MRI:购买圆二色性分光偏振仪,用于葛底斯堡学院本科生的研究和培训
批准号:
1725534
负责人:
Shelli Frey
金额:
$11.21万
依托单位:
依托单位国家:
美国
项目类别:
Standard Grant
财政年份:
2017
资助国家:
美国
项目状态:
已结题
起止时间:
2017-08-01 至 2020-07-31

项目摘要

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中文摘要
翻译
该奖项由主要研究仪器(MRI)和化学研究仪器(CRIF)项目支持。葛底斯堡学院的谢利·弗雷教授及其同事库尔特·安德森、凯瑟琳·比特纳和卢卡斯·汤普森获得了一台圆二色(CD)光谱仪。许多化学和生物分子是手性的(具有不可重叠的结构--比如我们的手)。在生物体中普遍存在的手性分子可以两种形式存在。这些形式可以描述为具有左手构象或右手构象。CD光谱仪可以确定存在哪种形式,或者是否存在这两种形式的混合物。光谱仪可以跟踪手性分子与另一个分子(配体)结合、重新排列其结构或(可能与药物或抗体)反应时的变化。因此,圆二色谱适合于探测蛋白质(或其他大分子结构)的结构或由于环境条件而引起的结构变化。圆二色谱已被广泛用于三种类型的测量:识别蛋白质的结构,研究蛋白质折叠和去折叠过程中的几何变化,以及确定结合相互作用和蛋白质去折叠所涉及的能量。这台光谱仪是本科生使用的。在接受使用这一重要工具的培训的同时,研究经验也为学生未来的职业生涯和医学和科学领域的高级学位做好了准备。NSF资助的STEM学者计划也使用了这种仪器,该计划培养了对科学领域感兴趣的不同背景的学生的社区意识。这种光谱偏振仪的获得为学生和教职员工开辟了新的研究途径,并帮助学生通过跨学科项目更多地了解科学的相互关联的本质。学生们可以在他们的课程中接触到这种仪器,最终导致研究人员准备进入研究生院或该科学领域的职业生涯。授予圆二色光谱仪旨在加强各个层面的研究和教育,特别是在下列领域:(A)开发小蛋白质中的钛和钒结合部位以确定二级结构并研究DNA切割;(B)将金纳米棒与静电吸附的多聚赖氨酸组装在一起,以了解分子结构如何转化为对手性纳米颗粒组装的控制;以及(C)研究核小体的折叠,以深入了解核小体中的DNA如何与体内其他生物分子相互作用。
英文摘要
This award is supported by the Major Research Instrumentation (MRI) and the Chemistry Research Instrumentation (CRIF) programs. Professor Shelli Frey from Gettysburg College and colleagues Kurt Andresen, Katherine Buettner and Lucas Thompson have acquired a circular dichroism (CD) spectrometer. Many chemical and biological molecules are chiral (having structures that are not superimposable - like our hands). Chiral molecules that are prevalent in living organisms can exist in two forms. These forms can be described as having left-handed or right-handed conformations. A CD spectrometer can determine which form or whether a mixture of both forms is present. The spectrometer can follow changes as the chiral molecule binds to another molecule (ligand), rearranges its structure, or reacts (perhaps with a drug or an antibody). Therefore, CD spectroscopy is suitable for probing protein (or other macromolecular) structures or changes to structures due to environmental conditions. CD spectroscopy has been widely used for three types of measurements: identifying the structure of proteins, studying the geometry changes during folding and unfolding of proteins, and determining the energies involved in binding interactions and protein unfolding. This spectrometer is used by undergraduates. While being trained to use this important tool, the research experience prepares the students for future careers and advanced degrees in medical and scientific fields. The instrument is also used by the NSF funded STEM Scholars program, which fosters a sense of community for students of diverse backgrounds with an interest in science fields. The acquisition of this spectropolarimeter opens new paths of research for students and faculty, and it helps students see more of the interconnected nature of science through the interdisciplinary projects. Students have access to this instrumentation in their courses, ultimately resulting in researchers prepared to enter graduate school or careers in the sciences.This award of a circular dichroism spectrometer is aimed at enhancing research and education at all levels, especially in areas such as:(a) developing titanium and vanadium binding sites in small proteins to determine secondary structure and study DNA cleavage, (b) assembling gold nanorods with electrostatically adsorbed poly-polyl-lysine to understand how molecular structure can translate into control over chiral nanoparticle assemblies, and (c) studying the folding of the nucleosome to give insight into how DNA in the nucleosome can interact with other biological molecules in vivo.
期刊论文(1)
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会议论文
DNA Cleavage by a De Novo Designed Protein–Titanium Complex
通过 De Novo 设计的蛋白质钛复合物进行 DNA 切割
DOI: 10.1021/acs.inorgchem.0c01707
发表时间: 2020
期刊: Inorganic Chemistry
影响因子: 4.6
作者: [Paredes, Alexander, Loh, Brittany M., Peduzzi, Olivia M., Reig, Amanda J., Buettner, Katherine M.]
通讯作者: Buettner, Katherine M.
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