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Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/3767

Title: Effects of Macromolecular Crowding on an Intrinsically Disordered Protein Characterized by Small-Angle Neutron Scattering with Contrast Matching
Authors: Johansen, D
Jeffries, CMJ
Hammouda, B
Trewhella, J
Goldenberg, DP
Keywords: Proteins
X-ray Diffraction
Nuclear Magnetic Resonance
Neutron Diffraction
In Vivo
Polymers
Issue Date: 16-Feb-2011
Publisher: Elsevier (Cell Press)
Citation: Johansen, D., Jeffries, C.M.J., Hammouda, B., Trewhella, J., Goldenberg, D.P. (2011). Effects of Macromolecular Crowding on an Intrinsically Disordered Protein Characterized by Small-Angle Neutron Scattering with Contrast Matching, Biophysical Journal, 100(4), 1120-1128.
Abstract: Small-angle neutron scattering was used to examine the effects of molecular crowding on an intrinsically disordered protein, the N protein of bacteriophage lambda, in the presence of high concentrations of a small globular protein, bovine pancreatic trypsin inhibitor (BPTI). The N protein was labeled with deuterium, and the D2O concentration of the solvent was adjusted to eliminate the scattering contrast between the solvent and unlabeled BPTI, leaving only the scattering signal from the unfolded protein. The scattering profile observed in the absence of BPTI closely matched that predicted for an ensemble of random conformations. With BPTI added to a concentration of 65 mg/mL, there was a clear change in the scattering profile representing an increase in the mass fractal dimension of the unfolded protein, from 1.7 to 1.9, as expected if crowding favors more compact conformations. The crowding protein also inhibited aggregation of the unfolded protein. At 130 mg/mL BPTI, however, the fractal dimension was not significantly different from that measured at the lower concentration, contrary to the predictions of models that treat the unfolded conformations as convex particles. These results are reminiscent of the behavior of polymers in concentrated melts, suggesting that these synthetic mixtures may provide useful insights into the properties of unfolded proteins under crowding conditions. © 2011, Cell Press
URI: http://dx.doi.org/10.1016/j.bpj.2011.01.020
http://apo.ansto.gov.au/dspace/handle/10238/3767
ISSN: 0006-3495
Appears in Collections:Journal Articles

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