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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
Statement of
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
Protein Conformation
Hydrogen-Ion Concentration
Scattering, Small Angle
Dynamic Light Scattering
Rights: © 2016 American Chemical Society
DOI: 10.1021/acs.jpcb.6b02475
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