ArticleProceedings of the National Academy of Sciences of the United States of America2023
Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 17 citations in OpenAlex.
- Enzymatic Encoding of Topology in an Intrinsically Disordered Single-Chain Protein.Angewandte Chemie (International ed. in English) · 2026Article
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Disordered but rhythmic-the role of intrinsic protein disorder in eukaryotic circadian timing.FEBS letters · 2026Review
- Optimized protein-water interactions and torsional refinements yield balanced atomistic protein force fields.Nature communications · 2025Article
- Single cell transcriptomics reveals enrichment of aggregation-prone alpha-synuclein isoforms across synucleinopathies.bioRxiv : the preprint server for biology · 2025Article
- Scale-free Spatio-temporal Correlations in Conformational Fluctuations of Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Intrinsic stiffness andPNAS nexus · 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
- Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Neurofilament Biophysics: From Structure to Biomechanics.Molecular biology of the cell · 2024Review
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- Cell phenotypes can be predicted from propensities of protein conformations.Current opinion in structural biology · 2023Review
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Short-range interactions and long-range contacts drive the 3D folding of structured proteins. The proteins' structure has a direct impact on their biological function. However, nearly 40% of the eukaryotes proteome is composed of intrinsically disordered proteins (IDPs) and protein regions that fluctuate between ensembles of numerous conformations. Therefore, to understand their biological function, it is critical to depict how the structural ensemble statistics correlate to the IDPs' amino acid sequence. Here, using small-angle X-ray scattering and time-resolved Förster resonance energy transfer (trFRET), we study the intramolecular structural heterogeneity of the neurofilament low intrinsically disordered tail domain (NFLt). Using theoretical results of polymer physics, we find that the Flory scaling exponent of NFLt subsegments correlates linearly with their net charge, ranging from statistics of ideal to self-avoiding chains. Surprisingly, measuring the same segments in the context of the whole NFLt protein, we find that regardless of the peptide sequence, the segments' structural statistics are more expanded than when measured independently. Our findings show that while polymer physics can, to some level, relate the IDP's sequence to its ensemble conformations, long-range contacts between distant amino acids play a crucial role in determining intramolecular structures. This emphasizes the necessity of advanced polymer theories to fully describe IDPs ensembles with the hope that it will allow us to model their biological function.
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