ArticleJournal of the American Chemical Society2010
A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 158 citations in OpenAlex.
- Protein Recognition of Linear and Cyclic Peptides of Homologous Sequences Implicated in the Aggregation of α-Synuclein.The journal of physical chemistry. B · 2025Article
- Wild-Type α-Synuclein Structure and Aggregation: A Comprehensive Coarse-Grained and All-Atom Molecular Dynamics Study.Journal of chemical information and modeling · 2024Article
- Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024Article
- PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins.Nucleic acids research · 2024Article
- Lipid-induced polymorphic amyloid fibril formation by α-synuclein.Protein science : a publication of the Protein Society · 2023Article
- Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.Nature communications · 2023Article
- α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023Review
- Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2023Article
- Improved Assessment of Globularity of Protein Structures and the Ellipsoid Profile of the Biological Assemblies from the PDB.Biomolecules · 2023Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Predicting molecular properties of α-synuclein using force fields for intrinsically disordered proteins.Proteins · 2023Article
- Optimizing Epitope Conformational Ensembles Using α-Synuclein Cyclic Peptide "Glycindel" Scaffolds: A Customized Immunogen Method for Generating Oligomer-Selective Antibodies for Parkinson's Disease.ACS chemical neuroscience · 2022Article
- Methylphenidate Analogues as a New Class of Potential Disease-Modifying Agents for Parkinson's Disease: Evidence from Cell Models and Alpha-Synuclein Transgenic Mice.Pharmaceutics · 2022Article
- Glycation of α-synuclein hampers its binding to synaptic-like vesicles and its driving effect on their fusion.Cellular and molecular life sciences : CMLS · 2022Article
- Intrinsically disordered proteins and proteins with intrinsically disordered regions in neurodegenerative diseases.Biophysical reviews · 2022Review
- Consequences of variability in α-synuclein fibril structure on strain biology.Acta neuropathologica · 2022Review
- Characterization of Amyloidogenic Peptide Aggregability in Helical Subspace.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Predictive Modeling of Neurotoxic α-Synuclein Polymorphs.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Implementing Complementary Approaches to Shape the Mechanism of α-Synuclein Oligomerization as a Model of Amyloid Aggregation.Molecules (Basel, Switzerland) · 2021Review
- A sequence-based method for predicting extant fold switchers that undergo α-helix ↔ β-strand transitions.Biopolymers · 2021Article
18 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
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Abstract
Partially folded proteins, characterized as exhibiting secondary structure elements with loose or absent tertiary contacts, represent important intermediates in both physiological protein folding and pathological protein misfolding. To aid in the characterization of the structural state(s) of such proteins, a novel structure calculation scheme is presented that combines structural restraints derived from pulsed EPR and NMR spectroscopy. The methodology is established for the protein alpha-synuclein (alphaS), which exhibits characteristics of a partially folded protein when bound to a micelle of the detergent sodium lauroyl sarcosinate (SLAS). By combining 18 EPR-derived interelectron spin label distance distributions with NMR-based secondary structure definitions and bond vector restraints, interelectron distances were correlated and a set of theoretical ensemble basis populations was calculated. A minimal set of basis structures, representing the partially folded state of SLAS-bound alphaS, was subsequently derived by back-calculating correlated distance distributions. A surprising variety of well-defined protein-micelle interactions was thus revealed in which the micelle is engulfed by two differently arranged antiparallel alphaS helices. The methodology further provided the population ratios between dominant ensemble structural states, whereas limitation in obtainable structural resolution arose from spin label flexibility and residual uncertainties in secondary structure definitions. To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound alphaS correlate with the degree of protein-induced departures from free micelle dimensions.
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