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Temperature-dependent solvation modulates the dimensions of disordered proteins
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Significance: A large number of naturally occurring proteins are now known to be unstructured under physiological conditions. Many of these intrinsically disordered proteins (IDPs) bind other biological macromolecules or ligands and are involved in important regulatory processes in the cell. For understanding the structural basis of these functional properties, it is essential to quantify the balance of interactions that modulate the heterogeneous conformational distributions of IDPs and unfolded proteins in general. In contrast to the behavior expected for simple polymers with temperature-independent intramolecular interactions, unfolded proteins become more compact when the temperature is raised. Here, we show that the temperature dependence of the interactions of the constituent amino acid residues with the aqueous solvent have a dominant effect on this behavior.
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“Proteins with very flexible conformations, such as intrinsically disordered proteins (IDP), are expected to have larger heat capacity than well-defined proteins.96–98”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [98]
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Metadata
- Authors
- Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B.
- Affiliations
- University of Zurich (CH)
- Lehigh University (US)
- National Institutes of Health (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2014-03-21
- Volume
- 111
- Issue
- 14
- Pages
- 5213-5218
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3986154
- OpenAlex
- W2113696142
- Cited by
- 192
- References
- 84
- Citations by year
- 2026: 7 · 2025: 17 · 2024: 10 · 2023: 16 · 2022: 14 · 2021: 20 · 2020: 14 · 2019: 22 · 2018: 14 · 2017: 16 · 2016: 15 · 2015: 20 · 2014: 7
- FWCI
- 7.92
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Keywords
- intrinsically disordered proteins, chain collapse, hydrophobic effect, solvation free energy, amino acid hydrophobicity, lambda repressor, protein unfolding
- MeSH terms
- Protein Conformation, Solubility, Temperature, Thermodynamics, Fluorescence Resonance Energy Transfer, Hydrophobic and Hydrophilic Interactions, Protein Unfolding
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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