FT-IR approaches on amyloid fibril structure
FT-IR approaches on amyloid fibril structure
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DOI：
10.1016/j.bbapap.2005.07.008
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发表时间：
2005-11-10
影响因子：
3.2
通讯作者：
Kitagawa, T
中科院分区：
文献类型：
--
作者：
Hiramatsu, H;Kitagawa, T
本文综述了傅里叶变换红外吸收光谱在蛋白质科学，特别是淀粉样原纤维结构方面的最新成就。它包括理论背景的简要说明、相关技术的描述以及原纤维结构分析的最新应用。关于理论背景，已经描述了根据肽主链中 C=O 振荡器之间的过渡偶极耦合对酰胺 I 的成功分析。该理论使我们能够估计蛋白质二级结构的含量。介绍了线性二色性测量、显微镜应用、同位素标记等相关实验技术。线性二色性测量带来了有关分子取向的直接信息，显微镜能够处理精心准备的颗粒，同位素标记技术允许我们以单残基分辨率进行结构讨论。综述了红外吸收光谱及相关技术在淀粉样蛋白纤维结构中的应用。将获得的模型与蛋白质天然结构进行比较。 (c) 2005 Elsevier B.V. 保留所有权利。
This review treats recent achievements of Fourier-transform infrared absorption spectroscopy on protein science, especially on amyloid fibril structure. It includes the brief explanation of theoretical background, description of related techniques, and recent applications to analysis of fibril structure. Concerns to theoretical background, successful analysis of Amide I in terms of transition dipole coupling between the C=O oscillators in peptide main chain has been described. The theory enables us to estimate a content of secondary structure in a protein. Related experimental techniques such as linear dichroism measurement, application of microscope, and isotope labeling, are introduced. The linear-dichroism measurement brings direct information on molecular orientation, microscope enables to treat a well-prepared particle, and isotope-label technique allows our structural discussion with one-residue resolution. Application of IR absorption spectroscopy and related techniques on amyloid fibril structure is reviewed. The model obtained is compared with protein native structure. (c) 2005 Elsevier B.V. All rights reserved.