1993/09/01 by Chris Colovos, Christos Colovos, Todd O. Yeates · 4 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Computer Science · #Computational Drug Discovery Methods #Crystallography and molecular interactions #Protein Structure and Dynamics
paper · pdf · doi:10.1002/pro.5560020916
openalex publication_date 1993/09/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/31
A novel method for differentiating between correctly and incorrectly determined regions of protein structures based on characteristic atomic interaction 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 (O). This leads to six different combinations of pairwise noncovalently bonded interactions (CC, CN, CO, NN, NO, and OO). 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.