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

Balu, R, Mata, J, Knott, R, Elvin, C, Hill, A, Choudhury, N and Dutta, N 2016, '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', Journal of Physical Chemistry B, vol. 120, no. 27, pp. 6490-6503.


Document type: Journal Article
Collection: Journal Articles

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(s) Balu, R
Mata, J
Knott, R
Elvin, C
Hill, A
Choudhury, N
Dutta, N
Year 2016
Journal name Journal of Physical Chemistry B
Volume number 120
Issue number 27
Start page 6490
End page 6503
Total pages 14
Publisher American Chemical Society
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.
Subject Atomic, Molecular, Nuclear, Particle and Plasma Physics not elsewhere classified
Biomaterials
Chemical Engineering not elsewhere classified
DOI - identifier 10.1021/acs.jpcb.6b02475
Copyright notice © 2016 American Chemical Society
ISSN 1520-6106
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