VERIFICATION OF PROTEIN STRUCTURES - PATTERNS OF NONBONDED ATOMIC INTERACTIONS
VERIFICATION OF PROTEIN STRUCTURES - PATTERNS OF NONBONDED ATOMIC INTERACTIONS
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DOI：
10.1002/pro.5560020916
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发表时间：
1993-09-01
期刊：
影响因子：
8
通讯作者：
YEATES, TO
中科院分区：
文献类型：
--
作者：
COLOVOS, C;YEATES, TO
描述了一种基于特征原子相互作用区分正确和错误确定的蛋白质结构区域的新方法。不同类型的原子在蛋白质中的分布是非随机的。建模错误导致不同原子类型的分布更加随机化，这可以通过统计方法与正确的分布区分开来。原子被分为三类：碳(C)、氮(N)和氧(0)。这导致了六种不同的成对非共价键相互作用的组合(CC、CN、CO、NN、NO和00)。在96个可靠蛋白质结构的数据库中，使用二次误差函数来表征来自九个残基滑动窗口的成对相互作用集。然后，通过分析来自每个窗口的非结合相互作用的模式，可以识别被错误信任或错误注册的候选蛋白质结构的区域。
A novel method for differentiating between correctly and incorrectly determined regions of protein structures based on characteristic atomic interactions is described. Different types of atoms are distributed nonrandomly with respect to each other in proteins. Errors in model building lead to more randomized distributions of the different atom types, which can be distinguished from correct distributions by statistical methods.Atoms are classified in one of three categories: carbon (C), nitrogen (N), and oxygen (0). This leads to six different combinations of pairwise noncovalently bonded interactions (CC, CN, CO, NN, NO, and 00). A quadratic error function is used to characterize the set of pairwise interactions from nine-residue sliding windows in a database of 96 reliable protein structures. Regions of candidate protein structures that are mistraced or misregistered can then be identified by analysis of the pattern of nonbonded interactions from each window.