ArticleProtein science : a publication of the Protein Society2011
Fractal dimension of an intrinsically disordered protein: small-angle X-ray scattering and computational study of the bacteriophage λ N protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 55 citations in OpenAlex.
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- Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin.The Biochemical journal · 2025Article
- A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Self-Diffusive Properties of the Intrinsically Disordered Protein Histatin 5 and the Impact of Crowding Thereon: A Combined Neutron Spectroscopy and Molecular Dynamics Simulation Study.The journal of physical chemistry. B · 2022Article
- Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins.The Journal of biological chemistry · 2021Article
- Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder.The journal of physical chemistry. B · 2020Review
- Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Emerging consensus on the collapse of unfolded and intrinsically disordered proteins in water.Current opinion in structural biology · 2020Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis.Progress in molecular biology and translational science · 2020Review
- Dynamical Oligomerisation of Histidine Rich Intrinsically Disordered ProteinS Is Regulated through Zinc-Histidine Interactions.Biomolecules · 2019Article
- Self-organization, entropy and allostery.Biochemical Society transactions · 2018Review
- Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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3 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Small-angle X-ray scattering (SAXS) was used to characterize the bacteriophage λ N protein, a 107 residue intrinsically disordered protein (IDP) that functions as a transcriptional antitermination factor. The SAXS data were used to estimate both the average radius of gyration and the fractal dimension, a measure of the protein's internal scaling properties, under a variety of solution conditions. In the absence of denaturants, the radius of gyration was 38 ± 3.5 Å and the fractal dimension was 1.76 ± 0.05, slightly larger than the value predicted for a well-solvated polymer with excluded volume (1.7). Neither the radius of gyration nor the fractal dimension changed significantly on the addition of urea, further indicating that the protein is extensively unfolded and well solvated in the absence of denaturant. The addition of NaCl or D(2) O was found to promote aggregation, but did not appear to affect the properties of the monomeric form. The experimental SAXS profiles were also compared with those predicted by a computational model for a random-coil polypeptide, with an adjustable solvation energy term. The experimental data were well fit to the model with the solvation energy close to zero. These results indicate that the λ N protein is among the more expanded members of the broad class of IDPs, most likely because of its high content of charged residues and a large net charge (+15 at neutral pH). The expanded nature of the conformational ensemble may play a role in facilitating the interactions of the protein with other components of the dynamic transcriptional complex.
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