ArticleProtein science : a publication of the Protein Society2016
Disorder transitions and conformational diversity cooperatively modulate biological function in proteins.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- An inducible amphipathic α-helix mediates subcellular targeting and membrane binding of RPE65.Life science alliance · 2023Article
- Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder.The journal of physical chemistry. B · 2020Review
- Experimentally-driven protein structure modeling.Journal of proteomics · 2020Review
- Investigation into Early Steps of Actin Recognition by the Intrinsically Disordered N-WASP Domain V.International journal of molecular sciences · 2019Article
- Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data.Biophysical journal · 2019Article
- Bioinformatics in Latin America and SoIBio impact, a tale of spin-off and expansion around genomes and protein structures.Briefings in bioinformatics · 2019Article
- Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model.Biophysical journal · 2018Article
- Large scale analysis of protein conformational transitions from aqueous to non-aqueous media.BMC bioinformatics · 2018Article
- Homology modeling in a dynamical world.Protein science : a publication of the Protein Society · 2017Article
- Conformational diversity analysis reveals three functional mechanisms in proteins.PLoS computational biology · 2017Article
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Authors and funding
6 authors.
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Abstract
Structural differences between conformers sustain protein biological function. Here, we studied in a large dataset of 745 intrinsically disordered proteins, how ordered-disordered transitions modulate structural differences between conformers as derived from crystallographic data. We found that almost 50% of the proteins studied show no transitions and have low conformational diversity while the rest show transitions and a higher conformational diversity. In this last subset, 60% of the proteins become more ordered after ligand binding, while 40% more disordered. As protein conformational diversity is inherently connected with protein function our analysis suggests differences in structure-function relationships related to order-disorder transitions.
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