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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography
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Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography

机译:通过超高分辨率中子蛋白质晶体学直接观察氢原子动力学和相互作用

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摘要

The 1.1 A, ultrahigh resolution neutron structure of hydrogen/ deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventional interactions are clearly defined, including a potential O-H...π interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C-H...O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 A ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data.
机译:据报道,氢/氘(H / D)交换的Crambin具有1.1 A的超高分辨率中子结构。 315个蛋白中有299个(即94.9%)的氢原子位置已通过实验得到,并通过核密度图解析。清楚地定义了许多非常规相互作用,包括水分子与残基Y44的芳环之间的潜在O-H ...π相互作用,以及许多潜在的C-H ... O氢键。 0.85 A超高分辨率X射线结构中不明确的氢键网络可以通过水分子的精确取向来解决。此外,所报道结构的高分辨率已使蛋白质中36个氘原子的各向异性描述成为可能。关于中子数据的分辨率,讨论了氢和氘原子在核密度图中的可见性。

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