Driving Forces in the Formation of Biocondensates of Highly Charged Proteins: A Thermodynamic Analysis of the Binary Complex Formation.

Biomolecules

Institut für Chemie und Biochemie, Freie Universität Berlin, Forschungsbau SupraFab, Altensteinstrasse 23a, 14195 Berlin, Germany.

Published: November 2024

AI Article Synopsis

  • The study focuses on the interaction between the positively charged linker histone H1 and the negatively charged chaperone prothymosin α (ProTα), highlighting their strong binding in physiological conditions.
  • The analysis employs a thermodynamic model that considers the influence of counterion release and hydration on the complex formation.
  • The findings reveal that the binding energy is primarily driven by the release of counterions from ProTα, while changes in water interactions and conformational constraints contribute to a significant negative change in free energy.

Article Abstract

A thermodynamic analysis of the binary complex formation of the highly positively charged linker histone H1 and the highly negatively charged chaperone prothymosin α (ProTα) is detailed. ProTα and H1 have large opposite net charges (-44 and +53, respectively) and form complexes at physiological salt concentrations with high affinities. The data obtained for the binary complex formation are analyzed by a thermodynamic model that is based on counterion condensation modulated by hydration effects. The analysis demonstrates that the release of the counterions mainly bound to ProTα is the main driving force, and effects related to water release play no role within the limits of error. A strongly negative Δ (=-0.87 kJ/(K mol)) is found, which is due to the loss of conformational degrees of freedom.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11592313PMC
http://dx.doi.org/10.3390/biom14111421DOI Listing

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