Cited by 192Protein Structure and DynamicsProtein Interaction Studies and Fluorescence AnalysisPhotochemistry and Electron Transfer Studies

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

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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Crossref · 10.1073/pnas.1313006111

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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)
Venue
Proceedings of the National Academy of Sciences
Published
2014-03-21
Volume
111
Issue
14
Pages
5213-5218
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
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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