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https://hdl.handle.net/2440/105110
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dc.contributor.author | Balu, R. | - |
dc.contributor.author | Mata, J. | - |
dc.contributor.author | Knott, R. | - |
dc.contributor.author | Elvin, C. | - |
dc.contributor.author | Hill, A. | - |
dc.contributor.author | Choudhury, N. | - |
dc.contributor.author | Dutta, N. | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | The Journal of Physical Chemistry B: Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter, 2016; 120(27):6490-6503 | - |
dc.identifier.issn | 1520-6106 | - |
dc.identifier.issn | 1520-5207 | - |
dc.identifier.uri | http://hdl.handle.net/2440/105110 | - |
dc.description.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. | - |
dc.description.statementofresponsibility | Rajkamal Balu, Jitendra P. Mata, Robert Knott, Christopher M. Elvin, Anita J. Hill, Namita R. Choudhury and Naba K. Dutta | - |
dc.language.iso | en | - |
dc.publisher | American Chemical Society | - |
dc.rights | © 2016 American Chemical Society | - |
dc.source.uri | http://dx.doi.org/10.1021/acs.jpcb.6b02475 | - |
dc.subject | Insect Proteins | - |
dc.subject | X-Ray Diffraction | - |
dc.subject | Temperature | - |
dc.subject | Protein Conformation | - |
dc.subject | Hydrogen-Ion Concentration | - |
dc.subject | Scattering, Small Angle | - |
dc.subject | Dynamic Light Scattering | - |
dc.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 | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1021/acs.jpcb.6b02475 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP1092678 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP120103537 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Dutta, N. [0000-0003-4800-1910] | - |
Appears in Collections: | Aurora harvest 8 Chemical Engineering publications |
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