奇异果甜蛋白的初步中子晶体学研究。
A preliminary neutron crystallographic study of thaumatin.
作者信息
Teixeira Susana C M, Blakeley Matthew P, Leal Ricardo M F, Mitchell Edward P, Forsyth V Trevor
机构信息
ILL-EMBL Deuteration Laboratory, Partnership for Structural Biology, 6 Rue Jules Horowitz, 38042 Grenoble, France.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):378-81. doi: 10.1107/S1744309108008294. Epub 2008 Apr 5.
A preliminary neutron crystallographic study of the sweet protein thaumatin is presented. Large hydrogenated crystals were prepared in deuterated crystallization buffer using the gel-acupuncture method. Data were collected to a resolution of 2 A on the LADI-III diffractometer at the Institut Laue Langevin (ILL). The results demonstrate the feasibility of a full neutron crystallographic analysis of this structure aimed at providing relevant information on the location of H atoms, the distribution of charge on the protein surface and localized water in the structure. This information will be of interest for understanding the specificity of thaumatin-receptor interactions and will contribute to further understanding of the molecular mechanisms underlying the perception of taste.
本文介绍了对甜味蛋白奇异果甜蛋白的初步中子晶体学研究。使用凝胶针刺法在氘化结晶缓冲液中制备了大型氢化晶体。在劳厄 - 朗之万研究所（ILL）的LADI - III衍射仪上收集了分辨率为2埃的数据。结果证明了对该结构进行全面中子晶体学分析的可行性，旨在提供有关氢原子位置、蛋白质表面电荷分布以及结构中局部水的相关信息。这些信息对于理解奇异果甜蛋白与受体相互作用的特异性将是有意义的，并将有助于进一步了解味觉感知背后的分子机制。
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