离子对蜘蛛丝蛋白重复结构域构象和动力学的影响：对可溶性和 β-折叠形成的影响。
Ion effects on the conformation and dynamics of repetitive domains of a spider silk protein: implications for solubility and β-sheet formation.
机构信息
Biomacromolecules Research Team, RIKEN Center for Sustainable Resource Scieences, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
出版信息
Chem Commun (Camb). 2019 Aug 13;55(66):9761-9764. doi: 10.1039/c9cc03538a.
PMID:31355386
Abstract
The effect of ions on the structure and dynamics of a spider silk protein is elucidated. Chaotropic ions prevent intra- and inter-molecular interactions on the repetitive domain, which are required to maintain the solubility, while kosmotropic ions promote hydrogen bond interactions in the glycine-rich region, which are a prerequisite for β-sheet formation.
摘要
阐明了离子对蜘蛛丝蛋白结构和动力学的影响。离液离子阻止重复结构域内和分子间的相互作用，这是维持蛋白质可溶性所必需的，而亲液离子促进甘氨酸丰富区域氢键相互作用，这是β-折叠形成的前提。
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