Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein rec1-resilin

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dc.contributor.authorBalu, Ren_AU
dc.contributor.authorKnott, RBen_AU
dc.contributor.authorCowieson, NPen_AU
dc.contributor.authorElvin, CMen_AU
dc.contributor.authorHill, AJen_AU
dc.contributor.authorChoudhury, NRen_AU
dc.contributor.authorDutta, NKen_AU
dc.date.accessioned2020-03-29T22:55:39Zen_AU
dc.date.available2020-03-29T22:55:39Zen_AU
dc.date.issued2015-06-04en_AU
dc.date.statistics2017-04-24en_AU
dc.description.abstractRec1-resilin is the first recombinant resilin-mimetic protein polymer, synthesized from exon-1 of the Drosophila melanogaster gene CG15920 that has demonstrated unusual multi-stimuli responsiveness in aqueous solution. Crosslinked hydrogels of Rec1-resilin have also displayed remarkable mechanical properties including near-perfect rubber-like elasticity. The structural basis of these extraordinary properties is not clearly understood. Here we combine a computational and experimental investigation to examine structural ensembles of Rec1-resilin in aqueous solution. The structure of Rec1-resilin in aqueous solutions is investigated experimentally using circular dichroism (CD) spectroscopy and small angle X-ray scattering (SAXS). Both bench-top and synchrotron SAXS are employed to extract structural data sets of Rec1-resilin and to confirm their validity. Computational approaches have been applied to these experimental data sets in order to extract quantitative information about structural ensembles including radius of gyration, pair-distance distribution function, and the fractal dimension. The present work confirms that Rec1-resilin is an intrinsically disordered protein (IDP) that displays equilibrium structural qualities between those of a structured globular protein and a denatured protein. The ensemble optimization method (EOM) analysis reveals a single conformational population with partial compactness. This work provides new insight into the structural ensembles of Rec1-resilin in solution. © 2017 Macmillan Publishers Limited, part of Springer Natureen_AU
dc.identifier.articlenumber10896en_AU
dc.identifier.citationBalu, R., Knott, R., Cowieson, N. P., Elvin, C. M., Hill, A. J., Choudhury, N. R., & Dutta, N. K. (2015). Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein rec1-resilin. Scientific Reports, 5. doi:10.1038/srep10896en_AU
dc.identifier.govdoc8123en_AU
dc.identifier.issn2045-2322en_AU
dc.identifier.journaltitleScientific Reportsen_AU
dc.identifier.urihttp://dx.doi.org/10.1038/srep10896en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/9294en_AU
dc.identifier.volume5en_AU
dc.language.isoenen_AU
dc.publisherSpringer Natureen_AU
dc.subjectPolymersen_AU
dc.subjectAqueous solutionsen_AU
dc.subjectProteinsen_AU
dc.subjectElasticityen_AU
dc.subjectGenesen_AU
dc.subjectDiagnosisen_AU
dc.subjectSpectroscopyen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectX-ray spectroscopyen_AU
dc.subjectDrosophilaen_AU
dc.subjectFruit fliesen_AU
dc.titleStructural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein rec1-resilinen_AU
dc.typeJournal Articleen_AU
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