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Quaternary structures of GroEL and naive-Hsp60 chaperonins in solution: a combined SAXS-MD study

机译:GroEL和朴素的Hsp60伴侣蛋白在溶液中的季结构:结合SAXS-MD研究

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摘要

The quaternary structures of bacterial GroEL and human naive-Hsp60 chaperonins in physiological conditions have been investigated by an innovative approach based on a combination of synchrotron Small Angle X-ray Scattering (SAXS) in-solution experiments and molecular dynamics (MD) simulations. Low-resolution SAXS experiments over large and highly symmetric oligomers are analyzed on the basis of the high-resolution structure of the asymmetric protein monomers, provided by MD. The results reveal remarkable differences between the solution and the crystallographic structure of GroEL and between the solution structures of GroEL and of its human homologue Hsp60.
机译:通过将同步加速器小角X射线散射(SAXS)溶液内实验与分子动力学(MD)模拟相结合的创新方法,研究了生理条件下细菌GroEL和人类朴素Hsp60伴侣蛋白的四级结构。在MD提供的不对称蛋白质单体的高分辨率结构的基础上,分析了在大型且高度对称的低聚物上的低分辨率SAXS实验。结果揭示了GroEL的溶液和晶体结构之间以及GroEL及其人类同源物Hsp60的溶液结构之间存在显着差异。

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