Chapter 5. Protein Structure Determination in Living Cells from NOE-derived Distance Restraints
Chapter 5. Protein Structure Determination in Living Cells from NOE-derived Distance Restraints
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第 5 章. 根据 NOE 衍生距离限制确定活细胞中的蛋白质结构
DOI：
10.1039/9781788013079-00063
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Ito Yutaka
中科院分区：
文献类型：
--
作者：
Ikeya Teppei;Guentert Peter;Ito Yutaka
在细胞内环境中，生物大分子在极端的分子拥挤条件下表达其生物学功能，其中与其他蛋白质、核酸、辅助因子、配体和各种其他小分子的特异性和非特异性相互作用发挥着重要作用。尽管生物大分子结构测定的体外方法、X射线晶体学、溶液核磁共振波谱和冷冻电子显微镜单颗粒分析为理解其生物活性的结构基础做出了重大贡献，但对生物大分子行为的详细体内观察仍然具有挑战性。针对活细胞样品的 NMR 光谱，细胞内 NMR，2-5 是目前在活生物系统中以原子分辨率观察蛋白质和核酸的唯一方法。
In an intracellular environment, bio-macromolecules express their biological functions under extreme molecular crowding conditions1 in which both specific and non-specific interactions with other proteins, nucleic acids, co-factors, ligands and various other small molecules play an important role. Although in vitro methods of structure determination of bio-macromolecules, X-ray crystallography, solution NMR spectroscopy, and single particle analysis with cryo-electron microscopy, have made significant contributions to understanding the structural bases of their biological activity, detailed in vivo observations of the behaviour of bio-macromolecules are still challenging. NMR spectroscopy targeting live cell samples, in-cell NMR, 2–5 is currently the only method for observing proteins and nucleic acids at atomic resolution in living biological systems.