Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin.
Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin.
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DOI：
10.1038/srep10896
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发表时间：
2015-06-04
影响因子：
4.6
通讯作者：
Dutta NK
中科院分区：
文献类型：
--
作者：
Balu R;Knott R;Cowieson NP;Elvin CM;Hill AJ;Choudhury NR;Dutta NK
Rec 1-resilin是第一个重组的resilin模拟蛋白聚合物，从果蝇基因CG 15920的外显子1合成，已被证明在水溶液中不寻常的多刺激响应性。Rec 1-节枝弹性蛋白的交联水凝胶也显示出显著的机械性能，包括近乎完美的橡胶样弹性。这些特殊性质的结构基础尚不清楚。在这里，我们结合联合收割机的计算和实验研究的结构合奏的Rec 1-节枝弹性蛋白在水溶液中。采用圆二色性（CD）光谱和小角X射线散射（SAXS）对Rec 1-节枝弹性蛋白在水溶液中的结构进行了实验研究。采用台式和同步辐射小角X射线散射技术提取Rec 1-resilin的结构数据集，并验证其有效性。计算方法已被应用到这些实验数据集，以提取定量信息的结构合奏，包括回转半径，对距离分布函数，和分形维数。目前的工作证实，Rec 1-节枝弹性蛋白是一种本质上无序的蛋白质（IDP），显示平衡结构的球状蛋白质和变性蛋白质之间的结构质量。系综优化方法（EOM）分析揭示了一个单一的构象人口与部分紧凑性。这项工作提供了新的洞察Rec 1-节枝弹性蛋白在解决方案的结构合奏。
Rec1-resilin is the first recombinant resilin-mimetic protein polymer, synthesized from exon-1 of the Drosophila melanogaster gene CG15920 that has demonstrated unusual multi-stimuli responsiveness in aqueous solution. Crosslinked hydrogels of Rec1-resilin have also displayed remarkable mechanical properties including near-perfect rubber-like elasticity. The structural basis of these extraordinary properties is not clearly understood. Here we combine a computational and experimental investigation to examine structural ensembles of Rec1-resilin in aqueous solution. The structure of Rec1-resilin in aqueous solutions is investigated experimentally using circular dichroism (CD) spectroscopy and small angle X-ray scattering (SAXS). Both bench-top and synchrotron SAXS are employed to extract structural data sets of Rec1-resilin and to confirm their validity. Computational approaches have been applied to these experimental data sets in order to extract quantitative information about structural ensembles including radius of gyration, pair-distance distribution function, and the fractal dimension. The present work confirms that Rec1-resilin is an intrinsically disordered protein (IDP) that displays equilibrium structural qualities between those of a structured globular protein and a denatured protein. The ensemble optimization method (EOM) analysis reveals a single conformational population with partial compactness. This work provides new insight into the structural ensembles of Rec1-resilin in solution.
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影响因子：
16.6
作者：
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通讯作者：
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