Work

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

Year: 2024

Type: 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 Δcp (=−0.87 kJ/(K mol)) is found, which is due to the loss of conformational degrees of freedom.

Source: Biomolecules

DOI: 10.3390/biom14111421

Author: Matthias Ballauff

Institution: Freie Universität Berlin

Language: English

Topic: Electrostatics and Colloid Interactions

Subfield: Physical and Theoretical Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: gold

Estimated APC paid: $3,069

Funder: Deutsche Forschungsgemeinschaft