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|Title:||Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein rec1-resilin|
Small angle scattering
|Citation:||Balu, 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/srep10896|
|Abstract:||Rec1-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 Nature|
|Gov't Doc #:||8123|
|Appears in Collections:||Journal Articles|
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