DADIMODO: a program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints
DADIMODO: a program for refining the structure of multidomain proteins and complexes against small-angle scattering data and NMR-derived restraints
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DOI：
10.1107/s0021889811035758
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发表时间：
2011-12-01
影响因子：
6.1
通讯作者：
Perez, Javier
中科院分区：
文献类型：
--
作者：
Evrard, Guillaume;Mareuil, Fabien;Perez, Javier
DADIMODO是一个程序，用于根据小角度X射线散射数据改进多结构域蛋白质或复合物的原子模型。域间距离和取向限制，如那些来自NMR测量，可以包括在优化过程中。虽然域结构主要保持刚性，但灵活的区域可以由用户定义。逐步通用的构象变化，由用户指定的，在一个随机优化算法，在蛋白质构象空间进行搜索循环应用。这种遗传算法的收敛性是由一个适应性强的选择压力驱动的。算法结构保证在优化的所有阶段都存在结构的物理上可接受的完整原子模型。图形用户界面确保用户友好的处理。
DADIMODO is a program for refining atomic models of multidomain proteins or complexes against small-angle X-ray scattering data. Interdomain distance and orientational restraints, such as those derived from NMR measurements, can be included in the optimization process. While domain structures are mainly kept rigid, flexible regions can be user defined. Stepwise generic conformational changes, specified by the user, are applied cyclically in a stochastic optimization algorithm that performs a search in the protein conformation space. The convergence for this genetic algorithm is driven by an adaptable selection pressure. The algorithmic structure guarantees that a physically acceptable full atomic model of the structure is present at all stages of the optimization. A graphical user interface ensures user-friendly handling.