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https://hdl.handle.net/2440/105110
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Type: | Journal article |
Title: | Effects of crowding and environment on the evolution of conformational ensembles of the multi-stimuli-responsive intrinsically disordered protein, Rec1-Resilin: a small-angle scattering investigation |
Author: | Balu, R. Mata, J. Knott, R. Elvin, C. Hill, A. Choudhury, N. Dutta, N. |
Citation: | The Journal of Physical Chemistry B: Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter, 2016; 120(27):6490-6503 |
Publisher: | American Chemical Society |
Issue Date: | 2016 |
ISSN: | 1520-6106 1520-5207 |
Statement of Responsibility: | Rajkamal Balu, Jitendra P. Mata, Robert Knott, Christopher M. Elvin, Anita J. Hill, Namita R. Choudhury and Naba K. Dutta |
Abstract: | In this study, we explore the overall structural ensembles and transitions of a biomimetic, multi-stimuli-responsive, intrinsically disordered protein (IDP), Rec1-resilin. The structural transition of Rec1-resilin with change in molecular crowding and environment is evaluated using small-angle neutron scattering and small-angle X-ray scattering. The quantitative analyses of the experimental scattering data using a combination of computational models allowed comprehensive description of the structural evolution, organization, and conformational ensembles of Rec1-resilin in response to the changes in concentration, pH, and temperature. Rec1-resilin in uncrowded solutions demonstrates the equilibrium intrinsic structure quality of an IDP with radius of gyration Rg ∼ 5 nm, and a scattering function for the triaxial ellipsoidal model best fit the experimental dataset. On crowding (increase in concentration >10 wt %), Rec1-resilin molecules exert intermolecular repulsive force of interaction, the Rg value reduces with a progressive increase in concentration, and molecular chains transform from a Gaussian coil to a fully swollen coil. It is also revealed that the structural organization of Rec1-resilin dynamically transforms from a rod (pH 2) to coil (pH 4.8) and to globular (pH 12) as a function of pH. The findings further support the temperature-triggered dual-phase-transition behavior of Rec1-resilin, exhibiting rod-shaped structural organization below the upper critical solution temperature (∼4 °C) and a large but compact structure above the lower critical solution temperature (∼75 °C). This work attempted to correlate unusual responsiveness of Rec1-resilin to the evolution of conformational ensembles. |
Keywords: | Insect Proteins X-Ray Diffraction Temperature Protein Conformation Hydrogen-Ion Concentration Scattering, Small Angle Dynamic Light Scattering |
Rights: | © 2016 American Chemical Society |
DOI: | 10.1021/acs.jpcb.6b02475 |
Grant ID: | http://purl.org/au-research/grants/arc/DP1092678 http://purl.org/au-research/grants/arc/DP120103537 |
Published version: | http://dx.doi.org/10.1021/acs.jpcb.6b02475 |
Appears in Collections: | Aurora harvest 8 Chemical Engineering publications |
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