Reynolds Christopher, Damerell David, Jones Susan
Department of Biochemistry, School of Life Sciences, John Maynard Smith Building, University of Sussex, Falmer, Brighton BN1 9QG, UK.
Bioinformatics. 2009 Feb 1;25(3):413-4. doi: 10.1093/bioinformatics/btn584. Epub 2008 Nov 11.
The PROTORP server analyses protein-protein associations in 3D structures. The server calculates a series of physical and chemical parameters of the protein interaction sites that contribute to the binding energy of the association. These parameters include, size and shape, intermolecular bonding, residue and atom composition and secondary structure contributions. The server is flexible, in that it allows users to analyse individual protein associations or large datasets of associations deposited in the PDB, or upload and analyse proprietary files. The properties calculated can be compared with parameter distributions for non-homologous datasets of different classes of protein associations provided on the server website. The server provides an efficient way of characterizing protein-protein associations of new or existing proteins, and a means of putting these values in the context of previously observed associations.
PROTORP服务器分析三维结构中的蛋白质-蛋白质相互作用。该服务器计算有助于相互作用结合能的蛋白质相互作用位点的一系列物理和化学参数。这些参数包括大小和形状、分子间键合、残基和原子组成以及二级结构贡献。该服务器具有灵活性，因为它允许用户分析单个蛋白质相互作用或沉积在蛋白质数据银行（PDB）中的大型相互作用数据集，或上传并分析专有文件。计算出的属性可以与服务器网站上提供的不同类别蛋白质相互作用的非同源数据集的参数分布进行比较。该服务器提供了一种有效表征新的或现有蛋白质的蛋白质-蛋白质相互作用的方法，以及一种将这些值置于先前观察到的相互作用背景下的手段。
