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用于蛋白质结构与动力学的紫外共振拉曼光谱标记物

Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics.

作者信息

Jakubek Ryan S, Handen Joseph, White Stephen E, Asher Sanford A, Lednev Igor K

机构信息

Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.

Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, New York 12222, USA.

出版信息

Trends Analyt Chem. 2018 Jun;103:223-229. doi: 10.1016/j.trac.2017.12.002. Epub 2017 Dec 11.

DOI:10.1016/j.trac.2017.12.002
PMID:32029956
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7003616/
Abstract

UV resonance Raman (UVRR) spectroscopy is a powerful tool for investigating the structure of biological molecules, such as proteins. Numerous UVRR spectroscopic markers that provide information on the structure and environment of the protein backbone and of amino acid side chains have recently been discovered. Combining these UVRR markers with hydrogen-deuterium exchange and advanced statistics is a powerful tool for studying protein systems, including the structure and formation mechanism of protein aggregates and amyloid fibrils. These techniques allow crucial new insights into the structure and dynamics of proteins, such as polyglutamine peptides, which are associated with 10 different neurodegenerative diseases. Here we summarize the spectroscopic structural markers recently developed and the important insights they provide.

摘要

紫外共振拉曼(UVRR)光谱是研究生物分子(如蛋白质)结构的有力工具。最近发现了许多能提供有关蛋白质主链和氨基酸侧链结构及环境信息的UVRR光谱标记物。将这些UVRR标记物与氢-氘交换及先进的统计学方法相结合,是研究蛋白质系统(包括蛋白质聚集体和淀粉样纤维的结构及形成机制)的有力工具。这些技术能让我们对与10种不同神经退行性疾病相关的蛋白质(如多聚谷氨酰胺肽)的结构和动力学有至关重要的新认识。在此,我们总结了最近开发的光谱结构标记物及其提供的重要见解。

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本文引用的文献

1
Monomeric Polyglutamine Structures That Evolve into Fibrils.单体多聚谷氨酰胺结构演变成纤维。
J Phys Chem B. 2017 Jun 22;121(24):5953-5967. doi: 10.1021/acs.jpcb.7b04060. Epub 2017 Jun 8.
2
Polyglutamine Fibrils: New Insights into Antiparallel β-Sheet Conformational Preference and Side Chain Structure.聚谷氨酰胺纤维:关于反平行β-折叠构象偏好和侧链结构的新见解
J Phys Chem B. 2016 Mar 31;120(12):3012-26. doi: 10.1021/acs.jpcb.5b11380. Epub 2016 Mar 18.
3
Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.谷氨酰胺和天冬酰胺侧链超共轭诱导的结构敏感振动
J Phys Chem B. 2015 Oct 15;119(41):13039-51. doi: 10.1021/acs.jpcb.5b07651. Epub 2015 Sep 30.
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Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review.利用拉曼光谱探究淀粉样纤维的结构与形成机制:综述
Analyst. 2015 Aug 7;140(15):4967-80. doi: 10.1039/c5an00342c.
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Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation.由pH升高驱动的HET-s(218-289)朊病毒原纤维的快速丝状超分子手性反转
J Phys Chem B. 2015 Jul 9;119(27):8521-5. doi: 10.1021/acs.jpcb.5b04779. Epub 2015 Jun 26.
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Dependence of Raman and resonance Raman intensities on sample self-absorption.
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UV resonance Raman and DFT studies of arginine side chains in peptides: insights into arginine hydration.紫外共振拉曼和密度泛函理论研究肽中的精氨酸侧链:精氨酸水合作用的深入了解。
J Phys Chem B. 2013 Jun 20;117(24):7145-56. doi: 10.1021/jp404030u. Epub 2013 Jun 5.
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Biochemistry. 2012 Jul 24;51(29):5822-30. doi: 10.1021/bi300551b. Epub 2012 Jul 12.