ArticleAnnual review of biophysics2018
Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.
Article in Annual review of biophysics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
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- Stability and Conformational Dynamics of Interferons: Structural Insights into the Urea- and Guanidinium Chloride-Induced Unfolding.ACS omega · 2026Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- NMR Dynamic View of the Destabilization of WW4 Domain by Chaotropic GdmCl and NaSCN.International journal of molecular sciences · 2024Article
- Direct prediction of intrinsically disordered protein conformational properties from sequence.Nature methods · 2024Article
- Sequence-Dependent Conformational Transitions of Disordered Proteins During Condensation.bioRxiv : the preprint server for biology · 2024Article
- Modulating hierarchical self-assembly in thermoresponsive intrinsically disordered proteins through high-temperature incubation time.Scientific reports · 2023Article
- Sequence-ensemble-function relationships for disordered proteins in live cells.bioRxiv : the preprint server for biology · 2023Article
- Sequence-ensemble-function relationships for disordered proteins in live cells.Research square · 2023Article
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
- FIREBALL: A tool to fit protein phase diagrams based on mean-field theories for polymer solutions.Biophysical journal · 2023Article
- The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins.The journal of physical chemistry. B · 2023Article
- The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.Biology · 2023Review
- The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins.bioRxiv : the preprint server for biology · 2023Article
- Effects of Sequence Composition, Patterning and Hydrodynamics on the Conformation and Dynamics of Intrinsically Disordered Proteins.International journal of molecular sciences · 2023Article
- Energy landscapes and heat capacity signatures for peptides correlate with phase separation propensity.QRB discovery · 2023Article
- Polymerization and Applications of Poly(methyl methacrylate)-Graphene Oxide Nanocomposites: A Review.ACS omega · 2022Review
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2 authors.
Funding
Abstract
Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like conformations. Additionally, they can fold into well-defined three-dimensional structures or remain partially or entirely disordered. Recent discoveries have shown that the tendency for proteins to collapse or remain expanded is not intrinsically coupled to their ability to fold. These observations suggest that proteins do not have to form compact globules in aqueous solutions. They can be intrinsically disordered, collapsed, or expanded, and even form well-folded, elongated structures. This ability to decouple collapse from folding is determined by the sequence details of proteins. In this review, we highlight insights gleaned from studies over the past decade. Using a polymer physics framework, we explain how the interplay among sidechains, backbone units, and solvent determines the driving forces for collapsed versus expanded states in aqueous solvents.
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