Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins.

ABSTRACT: Intrinsically disordered proteins are proteins whose native functional states represent ensembles of highly diverse conformations. Such ensembles are a challenge for quantitative structure comparisons because their conformational diversity precludes optimal superimposition of the atomic coordinates necessary for deriving common similarity measures such as the root mean-square deviation of these coordinates. Here, we introduce superimposition-free metrics that are based on computing matrices of the Cα-Cα distance distributions within ensembles and comparing these matrices between ensembles. Differences between two matrices yield information on the similarity between specific regions of the polypeptide, whereas the global structural similarity is captured by the root mean-square difference b

SUBMITTER: Lazar T 

PROVIDER: S-EPMC7300341 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature