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• W2034693855 abstract "Small-angle neutron scattering was used to study the effects of macromolecular crowding by two globular proteins, i.e., bovine pancreatic trypsin inhibitor and equine metmyoglobin, on the conformational ensemble of an intrinsically disordered protein, the N protein of bacteriophage λ. The λ N protein was uniformly labeled with 2H, and the concentrations of D2O in the samples were adjusted to match the neutron scattering contrast of the unlabeled crowding proteins, thereby masking their contribution to the scattering profiles. Scattering from the deuterated λ N was recorded for samples containing up to 0.12 g/mL bovine pancreatic trypsin inhibitor or 0.2 g/mL metmyoglobin. The radius of gyration of the uncrowded protein was estimated to be 30 Å and was found to be remarkably insensitive to the presence of crowders, varying by <2 Å for the highest crowder concentrations. The scattering profiles were also used to estimate the fractal dimension of λ N, which was found to be ∼1.8 in the absence or presence of crowders, indicative of a well-solvated and expanded random coil under all of the conditions examined. These results are contrary to the predictions of theoretical treatments and previous experimental studies demonstrating compaction of unfolded proteins by crowding with polymers such as dextran and Ficoll. A computational simulation suggests that some previous treatments may have overestimated the effective volumes of disordered proteins and the variation of these volumes within an ensemble. The apparent insensitivity of λ N to crowding may also be due in part to weak attractive interactions with the crowding proteins, which may compensate for the effects of steric exclusion." @default.
• W2034693855 created "2016-06-24" @default.
• W2034693855 creator A5032111372 @default.
• W2034693855 creator A5035195590 @default.
• W2034693855 date "2014-02-01" @default.
• W2034693855 modified "2023-09-30" @default.
• W2034693855 title "Minimal Effects of Macromolecular Crowding on an Intrinsically Disordered Protein: A Small-Angle Neutron Scattering Study" @default.
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• W2034693855 doi "https://doi.org/10.1016/j.bpj.2013.12.003" @default.
• W2034693855 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3945088" @default.
• W2034693855 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24559993" @default.
• W2034693855 hasPublicationYear "2014" @default.
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