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化学进展 2020, Vol. 32 Issue (8): 1231-1239 DOI: 10.7536/PC200536 前一篇   后一篇

• 综述 •

生物凝聚态物质的多层次结构表征

徐国华1, 成凯1, 王晨1, 李从刚1,**()   

  1. 1. 中国科学院精密测量科学与技术创新研究院 中国科学院生物磁共振分析重点实验室 波谱与原子分子物理国家重点实验室 武汉 430071
  • 收稿日期:2020-05-16 修回日期:2020-06-30 出版日期:2020-08-24 发布日期:2020-09-08
  • 通讯作者: 李从刚
  • 基金资助:
    国家自然科学基金项目(21874149); 国家自然科学基金项目(21925406); 国家自然科学基金项目(21904137); 国家自然科学基金项目(21505152)
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Multi-Hierarchical Structural Characterization of Biological Condensed Matters

Guohua Xu1, Kai Cheng1, Chen Wang1, Conggang Li1,**()   

  1. 1. Key Laboratory of Magnetic Resonance in Biological Syetems, CAS, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, China
  • Received:2020-05-16 Revised:2020-06-30 Online:2020-08-24 Published:2020-09-08
  • Contact: Conggang Li
  • About author:
    ** e-mail:
  • Supported by:
    National Natural Science Foundation of China(21874149); National Natural Science Foundation of China(21925406); National Natural Science Foundation of China(21904137); National Natural Science Foundation of China(21505152)

在生物体内到处都是由蛋白质、核酸和多糖等生物大分子构成的各种不同生物凝聚态物质,这些生物凝聚态物质形成不同的高级结构,执行不同的生物功能。获取这些生物凝聚态物质的高分辨结构是理解生命过程的重要途径。在离体环境中,获取高分辨结构的手段主要有X-射线晶体衍射、冷冻电镜和核磁共振等,而在活细胞内原位研究生物凝聚体的结构,核磁共振和化学交联质谱具有独特优势。本文总结了利用多种分析手段对生物凝聚态物质进行多层次结构表征的研究进展:包括简单纯化体系下的蛋白质分子机器,蛋白质纤维等;液-液相分离,大分子拥挤、限域等模拟细胞复杂环境下的生物大分子以及活细胞内生物大分子。

关键词： 生物凝聚态物质, 淀粉纤维, 结构, 液-液相分离, 活细胞

Biological Condensed Matters(BCM), which are composed of proteins, nucleic acids, polysaccharides and other Biological macromolecules, are ubiquitous inside the organism. These BCM form various structures to perform different function. The determination of the high-resolution structures of these BCM is importance of understanding the life process. In Vitro, X-ray crystallography, cryo-electron microscopy(cryo-EM) and nuclear magnetic resonance(NMR) are the main methods to obtain high-resolution structures, while nuclear magnetic resonance and chemical cross-linking mass spectrometry have unique advantages for in situ study of the structure of BCM in living cells. Here, we mainly summarize the research progress in the characterization of the structures of BCM: including purified molecular machines and fibrils, biomolecules under crowding, confinement, liquid-liquid phase separation and in living cells.

Contents

1 Introduction

2 The structural characterization of biomacromolecules in simple system

3 The structural characterization of biomacromolecules in liquid-liquid phase separation environment

4 The structural characterization of biomacromolecules in crowded and confined environments

5 The structural characterization of biomacromolecules in living cells

6 Conclusion and outlook

Key words: biological condensed matter(BCM), amyloid fiber, structure, liquid-liquid phase separation, living cells
()
表1 生物凝聚态物质的结构表征方法
Table 1 Structural characterization methods of BCM.
BCM Structural characterization methods
Proteins, nucleic acids and their complexes, molecular machines, chromatin (purified) Liquid NMR
X-ray
Cryo-EM
Amyloid fiber(purified) Solid-state NMR
Cryo-EM
Amyloid fiber in tissue Cryo-EM
Biomacromolecules in liquidliquid phase separation environment Liquid NMR
Biomacromolecules in crowded and confined environments Liquid NMR
Biomacromolecules in living cells Liquid NMR CXMS
图1 固体核磁共振解析的高分辨淀粉样多肽及蛋白质结构:(A)TTR(105-115)[15];(B)HET-s(218-289)[17];(C)Aβ42[16]
Fig.1 High-resolution amyloid peptides and protein structures determined by solid-state NMR.(A) Ensemble of 20 lowest energy structures(top) and ribbon representation of the structure of TTR(105-115) in amyloid fibrils[15].(B) Structure of HET-s(218-289) fibrils(five molecules of HET-s are shown). The fibril axis is indicated by an arrow[17].(C) Ribbon representation of the lowest energy structure showing the alignment of Aβ42dimers along the fibril axis. Only residues 15-42 are shown[16]. Reproduced by reference 15~17 with permission from Copyright(2004) National Academy of Sciences(NAS), U. S. A., American Association for the Advancement of Science(AAAS), and the American Chemical Society(ACS), respectively
图2 Ddx4形成相分离后仍处于无结构状态[48]:(A) 稀溶液中和相分离后的Ddx4的1H-15N HSQC 谱图的叠加;(B) 基于Ddx4主链归属所获得的δ2D 分数,该值体现Ddx4的二级结构倾向性,越接近于1表明形成该结构类型的倾向性越强
Fig.2
图3 Ub3A and TTHA1718在sf9 细胞中的结构[75]:(A)Ub3A 的结构;(B)TTHA1718的结构
Fig.3 Ub3A and TTHA1718 structures in living sf9 cells[75].(A) The Ub3A structure in sf9 cells(left). Ub3A structures in sf9 cells(blue) and in diluted solution(red), showing the backbone atoms(right). (B) The TTHA1718 structure in sf9 cells(left). TTHA1718 structures in sf9 cells(blue) and in diluted solution(red), showing the backbone atoms(right). Reproduced by reference 75 with permission from John Wiley and Sons
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