Visualising intrinsic disorder and conformational variation in protein ensembles.

摘要: Intrinsically disordered regions (IDRs) in proteins are still not well understood, but increasingly recognised as important key biological functions, diseases. IDRs often confound experimental structure determination—however, they present many of the available 3D structures, where exhibit a wide range conformations, from ill-defined and highly flexible to well-defined upon binding partner molecules, or post-translational modifications. Analysing such large conformational variations across ensembles structures can be complex difficult; our goal this paper is improve situation by augmenting traditional approaches (molecular graphics principal components) with methods human–computer interaction information visualisation, especially parallel coordinates. We new tool integrating these approaches, demonstrate how it dissect reveal functional insights into variation intrinsic disorder.