人转甲状腺素蛋白的初步中子晶体学研究。
Preliminary neutron crystallographic study of human transthyretin.
作者信息
Haupt Melina, Blakeley Matthew P, Teixeira Susana C M, Mason Sax A, Mitchell Edward P, Cooper Jonathan B, Forsyth V Trevor
机构信息
EPSAM, Keele University, Keele, Staffordshire ST5 5BG, England.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1428-31. doi: 10.1107/S1744309111036244. Epub 2011 Oct 27.
Abstract
Preliminary studies of perdeuterated crystals of human transthyretin (TTR) have been carried out using the LADI-III and D19 diffractometers at the Institut Laue-Langevin in Grenoble. The results demonstrate the feasibility of a full crystallographic analysis to a resolution of 2.0 Å using Laue diffraction and also illustrate the potential of using monochromatic instruments such as D19 for higher resolution studies where larger crystals having smaller unit cells are available. This study will yield important information on hydrogen bonding, amino-acid protonation states and hydration in the protein. Such information will be of general interest for an understanding of the factors that stabilize/destabilize TTR and for the design of ligands that may be used to counter TTR amyloid fibrillogenesis.
摘要
在格勒诺布尔的劳厄 - 朗之万研究所，使用LADI - III和D19衍射仪对人转甲状腺素蛋白（TTR）的全氘代晶体进行了初步研究。结果表明，使用劳厄衍射对分辨率为2.0 Å进行完整晶体学分析是可行的，同时也说明了在有更小晶胞的更大晶体可用时，使用诸如D19等单色仪器进行更高分辨率研究的潜力。这项研究将产生有关蛋白质中氢键、氨基酸质子化状态和水合作用的重要信息。这些信息对于理解稳定/不稳定TTR的因素以及设计可用于对抗TTR淀粉样纤维形成的配体具有普遍意义。
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