ArticleMolecular bioSystems2016
Folding propensity of intrinsically disordered proteins by osmotic stress.
Article in Molecular bioSystems, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Structural characterization of an intrinsically disordered protein complex using integrated small-angle neutron scattering and computing.Protein science : a publication of the Protein Society · 2023Article
- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- Full structural ensembles of intrinsically disordered proteins from unbiased molecular dynamics simulations.Communications biology · 2021Article
- Revealing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment.The journal of physical chemistry letters · 2020Article
- NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region.Biochemistry · 2019Article
- Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019Review
- Does water stress promote the proteome-wide adjustment of intrinsically disordered proteins in plants?Cell stress & chaperones · 2018Article
- Metabolic Profile of Oral Squamous Carcinoma Cell Lines Relies on a Higher Demand of Lipid Metabolism in Metastatic Cells.Frontiers in oncology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Proteins imparted with intrinsic disorder conduct a range of essential cellular functions. To better understand the folding and hydration properties of intrinsically disordered proteins (IDPs), we used osmotic stress to induce conformational changes in nuclear co-activator binding domain (NCBD) and activator for thyroid hormone and retinoid receptor (ACTR) separate from their mutual binding. Osmotic stress was applied by the addition of small and polymeric osmolytes, where we discovered that water contributions to NCBD folding always exceeded those for ACTR. Both NCBD and ACTR were found to gain α-helical structure with increasing osmotic stress, consistent with their folding upon NCBD/ACTR complex formation. Using small-angle neutron scattering (SANS), we further characterized NCBD structural changes with the osmolyte ethylene glycol. Here a large reduction in overall size initially occurred before substantial secondary structural change. By focusing on folding propensity, and linked hydration changes, we uncover new insights that may be important for how IDP folding contributes to binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.