确定富含半胱氨酸的蛋白质中的二硫键连接方式。
Pinpointing disulfide connectivities in cysteine-rich proteins.
作者信息
Bernardino K, Pinto M E F, Bolzani V S, de Moura A F, Batista Junior J M
机构信息
Department of Chemistry, Federal University of São Carlos - UFSCar, São Carlos, SP 13565-905, Brazil.
出版信息
Chem Commun (Camb). 2017 Jun 29;53(53):7337-7340. doi: 10.1039/c7cc02333b.
PMID:28508909
Abstract
A simple MD-based protocol is presented to accurately predict both the sequence and order of disulfide bond formation in proteins containing multiple cysteine residues. It provides a detailed description of their dynamical and structural features, which can be used to perform ensemble-averaged ECD calculations. Plant cyclotides are used as model compounds.
摘要
提出了一种基于分子动力学（MD）的简单方案，用于准确预测含有多个半胱氨酸残基的蛋白质中二硫键形成的序列和顺序。它详细描述了它们的动力学和结构特征，可用于进行系综平均电子圆二色（ECD）计算。植物环肽被用作模型化合物。
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