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Temperature-dependent solvation modulates the dimensions of disordered proteins

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Wuttke, René, Hofmann, Hagen, Nettels, Daniel, Borgia, Madeleine B., Mittal, Jeetain, Best, Robert B., Schuler, Benjamin·2014·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1313006111PMC PMC3986154

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Abstract

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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Salt‐Mediated Long‐Range Electrostatic Signature of Native Binding Surface Pre‐Organizes Bound‐Like Conformations of p53 C‐Terminal Intrinsically Disordered Region
Das, K., & Jana, B. (2026) · ChemPhysChem · doi:10.1002/cphc.70604

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: Hofmann, Hagen
Nettels, Daniel
Borgia, Madeleine B.
Mittal, Jeetain
Best, Robert B.
Schuler, Benjamin
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
DOI: 10.1073/pnas.1313006111
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

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Temperature-dependent solvation modulates the dimensions of disordered proteins

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