Please use this identifier to cite or link to this item: https://apo.ansto.gov.au/dspace/handle/10238/9294
Title: Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein rec1-resilin
Authors: Balu, R
Knott, RB
Cowieson, NP
Elvin, CM
Hill, AJ
Choudhury, NR
Dutta, NK
Keywords: Polymers
Aqueous solutions
Proteins
Elasticity
Genes
Diagnosis
Spectroscopy
Small angle scattering
X-ray spectrometry
Drosophila
Fruit flies
Issue Date: 4-Jun-2015
Publisher: Springer Nature
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
URI: http://dx.doi.org/10.1038/srep10896
http://apo.ansto.gov.au/dspace/handle/10238/9294
ISSN: 2045-2322
Appears in Collections:Journal Articles

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