ArticleBiophysical journal2014
Minimal effects of macromolecular crowding on an intrinsically disordered protein: a small-angle neutron scattering study.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 64 citations in OpenAlex.
- Core-shell model of the clusters of CPEB4 isoforms preceding liquid-liquid phase separation.Biophysical journal · 2024Article
- Structure of Single-Chain Nanoparticles under Crowding Conditions: A Random Phase Approximation Approach.Macromolecules · 2023Article
- Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.Protein science : a publication of the Protein Society · 2023Article
- Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.The journal of physical chemistry letters · 2022Article
- Homo-oligomerization of the human adenosine AeLife · 2021Article
- The Effects of Chain Length on the Structural Properties of Intrinsically Disordered Proteins in Concentrated Solutions.The journal of physical chemistry. B · 2020Article
- Depletion interactions modulate the binding between disordered proteins in crowded environments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein.Biochemistry · 2019Article
- Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein-Crowder Attraction.The journal of physical chemistry. B · 2018Article
- Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.Cellular and molecular life sciences : CMLS · 2018Review
- Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding.Biophysical journal · 2018Article
- Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering.Structure (London, England : 1993) · 2018Article
- Molecular simulations of cellular processes.Biophysical reviews · 2017Review
- Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.The journal of physical chemistry. B · 2017Article
- Protein folding, binding, and droplet formation in cell-like conditions.Current opinion in structural biology · 2017Review
- Folding propensity of intrinsically disordered proteins by osmotic stress.Molecular bioSystems · 2016Article
- Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments.Nature protocols · 2016Article
- Protein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.Biophysical journal · 2016Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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 (2)H, 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.
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