SANS simulation of aggregated protein in aqueous solution
SANS simulation of aggregated protein in aqueous solution
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DOI：
10.1016/j.nima.2008.11.121
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发表时间：
2009-02-21
影响因子：
1.4
通讯作者：
Fukunaga, Toshiharu
中科院分区：
文献类型：
--
作者：
Sugiyama, Masaaki;Hamada, Kei;Fukunaga, Toshiharu
基于蛋白质的晶体学数据，模拟了水溶液中聚集蛋白质的小角中子散射（SANS）。在获得目标蛋白质的晶体学数据后，将氢原子添加到数据中，然后用氘原子替换一些氢原子。用这些数据建立了结构模型，计算了它们的回转半径和SANS强度。将计算的SANS数据与实验数据进行比较，确定了最可能的结构。用这种分析方法，蛋白酶体α 7-亚基（PRS α）在水溶液中的聚集体结构进行了研究。三种结构模型。一个简单的单体和两种类型的晚餐，被认为是聚集结构的PRSa。分析表明，最好的妥协结构是晚餐，这与电子显微镜观察一致。(C)2008 Elsevier B. V.保留所有权利。
Small-angle neutron scattering (SANS) of aggregated protein in an aqueous solution is simulated based on the crystallographic data of the protein. After obtaining the crystallographic data of the target protein, hydrogen atoms are added to the data and then some hydrogen atoms are replaced with deuterium atoms. The structure models are made with this data and then their gyration radii and SANS intensities are calculated. Compared the calculated SANS data with the experimental one, the most probable structure is determined. With this analysis method, the aggregate structure of proteasome alpha 7-subunit (PRS alpha) in an aqueous solution was investigated. Three structural models. a simple monomer and two types of dinners, were supposed as the aggregated structure of PRSa. The analysis showed that the best compromised structure was the dinner, which was consistent with electron microscopy observation. (C) 2008 Elsevier B.V. All rights reserved.