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- W4362692232 endingPage "2602" @default.
- W4362692232 startingPage "2586" @default.
- W4362692232 abstract "Intrinsically disordered proteins (IDPs) lack a stable native conformation, making it challenging to characterize their structure and dynamics. Key topological motifs with fundamental biological relevance are often hidden in the conformational noise, eluding detection. Here, we develop a circuit topology toolbox to extract conformational patterns, critical contacts, and timescales from simulated dynamics of intrinsically disordered proteins. We follow the dynamics of IDPs by providing a smart low-dimensionality representation of their three-dimensional (3D) configuration in the topology space. Such an approach allows us to quantify topological similarity in dynamic systems, therefore providing a pipeline for structural comparison of IDPs." @default.
- W4362692232 created "2023-04-09" @default.
- W4362692232 creator A5006799562 @default.
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- W4362692232 creator A5029816593 @default.
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- W4362692232 creator A5079187925 @default.
- W4362692232 date "2023-04-07" @default.
- W4362692232 modified "2023-10-14" @default.
- W4362692232 title "Circuit Topology Approach for the Comparative Analysis of Intrinsically Disordered Proteins" @default.
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- W4362692232 doi "https://doi.org/10.1021/acs.jcim.3c00391" @default.
- W4362692232 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37026598" @default.
- W4362692232 hasPublicationYear "2023" @default.
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