Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin

Balu, R, Knott, R, Cowieson, N, Elvin, C, Hill, A, Choudhury, N and Dutta, N 2015, 'Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin', Scientific Reports, vol. 5, pp. 1-12.


Document type: Journal Article
Collection: Journal Articles

Title Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin
Author(s) Balu, R
Knott, R
Cowieson, N
Elvin, C
Hill, A
Choudhury, N
Dutta, N
Year 2015
Journal name Scientific Reports
Volume number 5
Start page 1
End page 12
Total pages 12
Publisher Nature Publishing Group
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.
Subject Biomaterials
Chemical Engineering not elsewhere classified
DOI - identifier 10.1038/srep10896
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ISSN 2045-2322
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