Anisotropy of fluctuation dynamics of proteins with an elastic network model
Anisotropy of fluctuation dynamics of proteins with an elastic network model
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DOI：
10.1016/s0006-3495(01)76033-x
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发表时间：
2001-01-01
影响因子：
3.4
通讯作者：
Bahar, I
中科院分区：
文献类型：
--
作者：
Atilgan, AR;Durell, SR;Bahar, I
关于蛋白质的天然构象的波动已被证明是适当地复制与一个简单的弹性网络模型，它已显示出良好的协议与许多不同的性质，为各种各样的蛋白质。该标量模型简单地研究结构中单个残基的运动幅度。为了进一步使用弹性模型方法来开发蛋白质机制的细节，扩展该模型以包括单个残基波动方向的附加细节变得至关重要。在本文中，提出了一种新的工具，用于此目的，并施加到视黄醇结合蛋白，这表明增强的灵活性，在该地区的进入配体结合位点和蛋白质的一部分结合到其载体蛋白。
Fluctuations about the native conformation of proteins have proven to be suitably reproduced with a simple elastic network model, which has shown excellent agreement with a number of different properties for a wide variety of proteins. This scalar model simply investigates the magnitudes of motion of individual residues in the structure. To use the elastic model approach further for developing the details of protein mechanisms, it becomes essential to expand this model to include the added details of the directions of individual residue fluctuations. In this paper a new tool is presented for this purpose and applied to the retinol-binding protein, which indicates enhanced flexibility in the region of entry to the ligand binding site and for the portion of the protein binding to its carrier protein.