Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching

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dc.contributor.authorJohansen, Den_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorHammouda, Ben_AU
dc.contributor.authorTrewhella, Jen_AU
dc.contributor.authorGoldenberg, DPen_AU
dc.date.accessioned2011-09-22T04:20:22Zen_AU
dc.date.available2011-09-22T04:20:22Zen_AU
dc.date.issued2011-02-16en_AU
dc.date.statistics2011-09-22en_AU
dc.description.abstractSmall-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 Pressen_AU
dc.identifier.citationJohansen, 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. doi:10.1016/j.bpj.2011.01.020en_AU
dc.identifier.govdoc3444en_AU
dc.identifier.issn0006-3495en_AU
dc.identifier.issue4en_AU
dc.identifier.journaltitleBiophysical Journalen_AU
dc.identifier.pagination1120-1128en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.bpj.2011.01.020en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/3767en_AU
dc.identifier.volume100en_AU
dc.language.isoenen_AU
dc.publisherElsevier (Cell Press)en_AU
dc.subjectProteinsen_AU
dc.subjectX-ray diffractionen_AU
dc.subjectNuclear magnetic resonanceen_AU
dc.subjectNeutron diffractionen_AU
dc.subjectIn vivoen_AU
dc.subjectPolymersen_AU
dc.titleEffects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matchingen_AU
dc.typeJournal Articleen_AU
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