Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/4990
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dc.contributor.authorHazra, Jagadish Prasad-
dc.date.accessioned2023-08-21T15:57:41Z-
dc.date.available2023-08-21T15:57:41Z-
dc.date.issued2022-
dc.identifier.citationJournal of Biomolecular Structure and Dynamics,2138552.en_US
dc.identifier.urihttps://doi.org/10.1080/07391102.2022.2138552-
dc.identifier.urihttp://hdl.handle.net/123456789/4990-
dc.descriptionOnly IISER Mohali authors are available in the record.en_US
dc.description.abstractIntrinsically disordered regions in proteins have been functionally linked to the protein–protein interactions and genesis of several membraneless organelles. Depending on their residual makeup, hydrophobicity or charge distribution they may remain in extended form or may assume certain conformations upon biding to a partner protein or peptide. The present work investigates the distribution and potential roles of disordered regions in the integral proteins of 1,2-propanediol utilization microcompartments. We use bioinformatics tools to identify the probable disordered regions in the shell proteins and enzyme of the 1,2-propanediol utilization microcompartment. Using a combination of computational modelling and biochemical techniques we elucidate the role of disordered terminal regions of a major shell protein and enzyme. Our findings throw light on the importance of disordered regions in the self-assembly, providing flexibility to shell protein and mediating its interaction with a native enzyme.en_US
dc.language.isoen_USen_US
dc.publisherTaylor and Francis Groupen_US
dc.subjectshell proteins and functionen_US
dc.subjectshell–enzyme interactionsen_US
dc.subject1,2-propanediol utilization microcompartmenten_US
dc.titleDisordered regions endow structural flexibility to shell proteins and function towards shell–enzyme interactions in 1,2-propanediol utilization microcompartmenten_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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