ArticleProtein science : a publication of the Protein Society2014
A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed.
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- Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- α-Synuclein Pathology in Synucleinopathies: Mechanisms, Biomarkers, and Therapeutic Challenges.International journal of molecular sciences · 2025Review
- Local structure propensities in disordered proteins from cross-correlated NMR spin relaxation.Journal of biomolecular NMR · 2025Article
- Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein.Journal of the American Chemical Society · 2025Article
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023Article
- The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.RSC advances · 2023Review
- Incorporation of DThe journal of physical chemistry. B · 2022Article
- Low-resolution description of the conformational space for intrinsically disordered proteins.Scientific reports · 2022Article
- IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States.The journal of physical chemistry. A · 2022Article
- Global Structure of the Intrinsically Disordered Protein Tau Emerges from Its Local Structure.JACS Au · 2022Article
- Thermodynamics and kinetics of the amyloid-β peptide revealed by Markov state models based on MD data in agreement with experiment.Chemical science · 2021Article
- Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Putative second hit rare genetic variants in families with seemingly GBA-associated Parkinson's disease.NPJ genomic medicine · 2021Article
- Detecting anisotropic segmental dynamics in disordered proteins by cross-correlated spin relaxation.Magnetic resonance (Gottingen, Germany) · 2021Article
- Comprehensive Structural and Thermodynamic Analysis of Prefibrillar WT α-Synuclein and Its G51D, E46K, and A53T Mutants by a Combination of Small-Angle X-ray Scattering and Variational Bayesian Weighting.Journal of chemical information and modeling · 2020Article
- A Unified De Novo Approach for Predicting the Structures of Ordered and Disordered Proteins.The journal of physical chemistry. B · 2020Article
- A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities.Journal of biomolecular NMR · 2020Article
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6 authors.
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Abstract
α-Synuclein is an intrinsically disordered protein of 140 residues that switches to an α-helical conformation upon binding phospholipid membranes. We characterize its residue-specific backbone structure in free solution with a novel maximum entropy procedure that integrates an extensive set of NMR data. These data include intraresidue and sequential H(N) − H(α) and H(N) − H(N) NOEs, values for (3) JHNHα, (1) JHαCα, (2) JCαN, and (1) JCαN, as well as chemical shifts of (15)N, (13)C(α), and (13)C' nuclei, which are sensitive to backbone torsion angles. Distributions of these torsion angles were identified that yield best agreement to the experimental data, while using an entropy term to minimize the deviation from statistical distributions seen in a large protein coil library. Results indicate that although at the individual residue level considerable deviations from the coil library distribution are seen, on average the fitted distributions agree fairly well with this library, yielding a moderate population (20-30%) of the PPII region and a somewhat higher population of the potentially aggregation-prone β region (20-40%) than seen in the database. A generally lower population of the αR region (10-20%) is found. Analysis of (1)H − (1)H NOE data required consideration of the considerable backbone diffusion anisotropy of a disordered protein.
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