A protein structural study based on the centrality analysis of protein sequence feature networks.

In this paper, we use network approaches to analyze the relations between protein sequence features for the top hierarchical classes of CATH and SCOP. We use fundamental connectivity measures such as correlation (CR), normalized mutual information rate (nMIR), and transfer entropy (TE) to analyze th...

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Main Authors: Xiaogeng Wan, Xinying Tan
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2021-01-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0248861&type=printable
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author Xiaogeng Wan
Xinying Tan
author_facet Xiaogeng Wan
Xinying Tan
author_sort Xiaogeng Wan
collection DOAJ
description In this paper, we use network approaches to analyze the relations between protein sequence features for the top hierarchical classes of CATH and SCOP. We use fundamental connectivity measures such as correlation (CR), normalized mutual information rate (nMIR), and transfer entropy (TE) to analyze the pairwise-relationships between the protein sequence features, and use centrality measures to analyze weighted networks constructed from the relationship matrices. In the centrality analysis, we find both commonalities and differences between the different protein 3D structural classes. Results show that all top hierarchical classes of CATH and SCOP present strong non-deterministic interactions for the composition and arrangement features of Cystine (C), Methionine (M), Tryptophan (W), and also for the arrangement features of Histidine (H). The different protein 3D structural classes present different preferences in terms of their centrality distributions and significant features.
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issn 1932-6203
language English
publishDate 2021-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj-art-614dd598f8fc45dba5b0f0931d74cf212025-08-20T02:55:31ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01163e024886110.1371/journal.pone.0248861A protein structural study based on the centrality analysis of protein sequence feature networks.Xiaogeng WanXinying TanIn this paper, we use network approaches to analyze the relations between protein sequence features for the top hierarchical classes of CATH and SCOP. We use fundamental connectivity measures such as correlation (CR), normalized mutual information rate (nMIR), and transfer entropy (TE) to analyze the pairwise-relationships between the protein sequence features, and use centrality measures to analyze weighted networks constructed from the relationship matrices. In the centrality analysis, we find both commonalities and differences between the different protein 3D structural classes. Results show that all top hierarchical classes of CATH and SCOP present strong non-deterministic interactions for the composition and arrangement features of Cystine (C), Methionine (M), Tryptophan (W), and also for the arrangement features of Histidine (H). The different protein 3D structural classes present different preferences in terms of their centrality distributions and significant features.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0248861&type=printable
spellingShingle Xiaogeng Wan
Xinying Tan
A protein structural study based on the centrality analysis of protein sequence feature networks.
PLoS ONE
title A protein structural study based on the centrality analysis of protein sequence feature networks.
title_full A protein structural study based on the centrality analysis of protein sequence feature networks.
title_fullStr A protein structural study based on the centrality analysis of protein sequence feature networks.
title_full_unstemmed A protein structural study based on the centrality analysis of protein sequence feature networks.
title_short A protein structural study based on the centrality analysis of protein sequence feature networks.
title_sort protein structural study based on the centrality analysis of protein sequence feature networks
url https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0248861&type=printable
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AT xinyingtan aproteinstructuralstudybasedonthecentralityanalysisofproteinsequencefeaturenetworks
AT xiaogengwan proteinstructuralstudybasedonthecentralityanalysisofproteinsequencefeaturenetworks
AT xinyingtan proteinstructuralstudybasedonthecentralityanalysisofproteinsequencefeaturenetworks