ArticleScientific reports2019
Fast NMR method to probe solvent accessibility and disordered regions in proteins.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Zika virus capsid protein closed structure modulates binding to host lipid systems.Protein science : a publication of the Protein Society · 2024Article
- Dengue Virus Capsid Protein Facilitates Genome Compaction and Packaging.International journal of molecular sciences · 2023Article
- TOAC spin-labeled peptides tailored for DNP-NMR studies in lipid membrane environments.Biophysical journal · 2021Article
- Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts.Biomolecules · 2021Article
- Computational Prediction of Intrinsically Disordered Proteins Based on Protein Sequences and Convolutional Neural Networks.Computational intelligence and neuroscience · 2021Article
- Structural and Functional Properties of the Capsid Protein of Dengue and RelatedInternational journal of molecular sciences · 2019Article
- Dengue Virus Capsid Protein Interaction With Nucleic Acids.BioFactors (Oxford, England)Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
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Abstract
Understanding protein structure and dynamics, which govern key cellular processes, is crucial for basic and applied research. Intrinsically disordered protein (IDP) regions display multifunctionality via alternative transient conformations, being key players in disease mechanisms. IDP regions are abundant, namely in small viruses, allowing a large number of functions out of a small proteome. The relation between protein function and structure is thus now seen from a different perspective: as IDP regions enable transient structural arrangements, each conformer can play different roles within the cell. However, as IDP regions are hard and time-consuming to study via classical techniques (optimized for globular proteins with unique conformations), new methods are required. Here, employing the dengue virus (DENV) capsid (C) protein and the immunoglobulin-binding domain of streptococcal protein G, we describe a straightforward NMR method to differentiate the solvent accessibility of single amino acid N-H groups in structured and IDP regions. We also gain insights into DENV C flexible fold region biological activity. The method, based on minimal pH changes, uses the well-established
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