ArticleChemphyschem : a European journal of chemical physics and physical chemistry2015
Forced folding of a disordered protein accesses an alternative folding landscape.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- A Thermodynamic Atlas of Proteomes Reveals Energetic Innovation across the Tree of Life.Molecular biology and evolution · 2022Article
- The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than milliseconds.Structure (London, England : 1993) · 2021Article
- Defining the Neuropathological Aggresome acrossThe journal of physical chemistry. B · 2021Review
- Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid-Liquid Phase Separation.Molecules (Basel, Switzerland) · 2020Article
- Similar Yet Different-Structural and Functional Diversity amongInternational journal of molecular sciences · 2020Article
- New technologies to analyse protein function: an intrinsic disorder perspective.F1000Research · 2020Review
- Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins.Biomolecules · 2019Review
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- Untangling the Conformational Polymorphism of Disordered Proteins Associated With Neurodegeneration at the Single-Molecule Level.Frontiers in molecular neuroscience · 2019Review
- A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation.Biochemistry · 2018Article
- Direct Single-Molecule Observation of Sequential DNA Bending Transitions by the Sox2 HMG Box.International journal of molecular sciences · 2018Article
- Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins.Biomolecules · 2018Review
- Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.Biophysical journal · 2018Article
- Multicolor protein FRET with tryptophan, selective coumarin-cysteine labeling, and genetic acridonylalanine encoding.Chemical communications (Cambridge, England) · 2017Article
- Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules.Biochemistry · 2017Article
- Folding propensity of intrinsically disordered proteins by osmotic stress.Molecular bioSystems · 2016Article
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Intrinsically disordered proteins (IDPs) are involved in diverse cellular functions. Many IDPs can interact with multiple binding partners, resulting in their folding into alternative ligand-specific functional structures. For such multi-structural IDPs, a key question is whether these multiple structures are fully encoded in the protein sequence, as is the case in many globular proteins. To answer this question, here we employed a combination of single-molecule and ensemble techniques to compare ligand-induced and osmolyte-forced folding of α-synuclein. Our results reveal context-dependent modulation of the protein's folding landscape, suggesting that the codes for the protein's native folds are partially encoded in its primary sequence, and are completed only upon interaction with binding partners. Our findings suggest a critical role for cellular interactions in expanding the repertoire of folds and functions available to disordered proteins.
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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.