Aydinkal, R.M.Bağcı, Elife Zerrin2022-05-112022-05-1120180887-3585https://doi.org/10.1002/prot.25459https://hdl.handle.net/20.500.11776/4634Intrinsically disordered proteins (IDPs)/regions do not have well-defined secondary and tertiary structures, however, they are functional and it is critical to gain a deep understanding of their residue packing. The shape distributions methodology, which is usually utilized in pattern recognition, clustering, and classification studies in computer science, may be adopted to study the residue packing of the proteins. In this study, shape distributions of the globular proteins and IDPs were obtained to shed light on the residue packing of their structures. The shape feature that was used is the sphericity of tetrahedra obtained by Delaunay Tessellation of points of C? coordinates. Then the sphericity probability distributions were compared by using Principal Component Analysis. This computational structural study shows that the set of IDPs constitute a more diverse set than the set of globular proteins in terms of the geometrical properties of their network structures. © 2018 Wiley Periodicals, Inc.en10.1002/prot.25459info:eu-repo/semantics/closedAccessDelaunay Tessellationintrinsically disordered proteinsPrincipal Component Analysisresidue packingshape distributionssphericity of tetrahedraglobular proteinintrinsically disordered proteinintrinsically disordered proteinArticlecontrolled studyphysical parametersprincipal component analysispriority journalprotein functionprotein structureresidue packingsphericityanimalchemistryhumanmolecular modelprobabilityprotein databaseprotein secondary structureAnimalsDatabases, ProteinHumansIntrinsically Disordered ProteinsModels, MolecularPrincipal Component AnalysisProbabilityProtein Structure, SecondaryArticle864434438Q3WOS:0004265971000062-s2.0-8504118999529341251Q1