Neutron protein crystallography: beyond the folding structure of biological macromolecules.
Neutron protein crystallography: beyond the folding structure of biological macromolecules.
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DOI：
10.1107/s0108767307043498
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
N. Niimura;R. Bau
中科院分区：
文献类型：
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作者：
N. Niimura;R. Bau
中子衍射提供了一种直接定位蛋白质中氢原子的实验方法，这是一种补充超高分辨率X射线衍射的技术。日本、法国和美国建造了三种不同类型的生物大分子中子衍射仪，用于测定蛋白质的晶体结构，分辨率可达1.5-2.5A。从这些研究中得到了与蛋白质中H原子位置和水化模式有关的结果。这些例子包括氢键的几何细节，H原子在酶活性中的作用，CH3构型，蛋白质和寡核苷酸中的H/D交换，以及水化结构的动力学行为，所有这些都已从这些结构结果中提取并进行了综述。还描述了其他技术，如大单晶的生长和蛋白质中氢和水合作用的数据库。
Neutron diffraction provides an experimental method of directly locating H atoms in proteins, a technique complementary to ultra-high-resolution X-ray diffraction. Three different types of neutron diffractometers for biological macromolecules have been constructed in Japan, France and the USA, and they have been used to determine the crystal structures of proteins up to resolution limits of 1.5-2.5 A. Results relating to H-atom positions and hydration patterns in proteins have been obtained from these studies. Examples include the geometrical details of hydrogen bonds, the role of H atoms in enzymatic activity, CH3 configuration, H/D exchange in proteins and oligonucleotides, and the dynamical behavior of hydration structures, all of which have been extracted from these structural results and reviewed. Other techniques, such as the growth of large single crystals and a database of hydrogen and hydration in proteins, are described.