ArticleJournal of the American Chemical Society2009
Prediction of the rotational tumbling time for proteins with disordered segments.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
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- Promiscuous and multivalent interactions between Eps15 and partner protein Dab2 generate a complex interaction network.Nature communications · 2025Article
- AbMelt: Learning antibody thermostability from molecular dynamics.Biophysical journal · 2024Article
- Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation.Journal of the American Chemical Society · 2024Article
- SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.Nucleic acids research · 2023Article
- Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets.Nature communications · 2023Article
- Sequential Two-Photon Delayed Fluorescence Anisotropy for Macromolecular Size Determination.The journal of physical chemistry. B · 2023Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- Enthalpy-Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners.Biomolecules · 2021Article
- β-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding.Antimicrobial agents and chemotherapy · 2020Article
- Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65).Protein science : a publication of the Protein Society · 2019Article
- Perspective: the essential role of NMR in the discovery and characterization of intrinsically disordered proteins.Journal of biomolecular NMR · 2019Review
- Molecular recognition of ubiquitin and Lys63-linked diubiquitin by STAM2 UIM-SH3 dual domain: the effect of its linker length and flexibility.Scientific reports · 2019Article
- Article
- The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions.The Journal of biological chemistry · 2017Article
- Molecular Cross-Talk between Nonribosomal Peptide Synthetase Carrier Proteins and Unstructured Linker Regions.Chembiochem : a European journal of chemical biology · 2017Article
- Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases.The Journal of biological chemistry · 2017Article
- Characterizing Aciniform Silk Repetitive Domain Backbone Dynamics and Hydrodynamic Modularity.International journal of molecular sciences · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
For well-structured, rigid proteins, the prediction of rotational tumbling time (tau(c)) using atomic coordinates is reasonably accurate, but is inaccurate for proteins with long unstructured sequences. Under physiological conditions, many proteins contain long disordered segments that play important regulatory roles in fundamental biological events including signal transduction and molecular recognition. Here we describe an ensemble approach to the boundary element method that accurately predicts tau(c) for such proteins by introducing two layers of molecular surfaces whose correlated velocities decay exponentially with distance. Reliable prediction of tau(c) will help to detect intra- and intermolecular interactions and conformational switches between more ordered and less ordered states of the disordered segments. The method has been extensively validated using 12 reference proteins with 14 to 103 disordered residues at the N- and/or C-terminus and has been successfully employed to explain a set of published results on a system that incorporates a conformational switch.
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