Low-Dimensional Energetic Landscape Governing Ca2⁺ Binding in Troponin C.

Authors

Abdul Basit

Published in

Biophysical journal. Sep 04, 2026. Epub Sep 04, 2026.

Abstract

Ca²⁺ binding regulates muscle contraction through coupled structural and dynamical mechanisms, yet a unified description of mutation-induced perturbations in binding energetics remains incomplete. Mutational effects on proteins are often high-dimensional and difficult to interpret mechanistically. Here, we develop a physically interpretable low-dimensional reaction coordinate that captures coordination environment, electrostatic features, and dynamical coupling. Structural, electrostatic, and dynamical descriptors correlate with experimental binding free energies with Pearson coefficients of Rp = 0.83, 0.83, and 0.85, respectively. Integration of these domains improves agreement with experiment (Rp = 0.90), indicating substantial dimensional compression of the underlying descriptor space. This framework provides a physically grounded description of how mutations reshape Ca2+ binding energetics in a minimal EF-hand system.

PMID:
42698210
Bibliographic data and abstract were imported from PubMed on 05 Sep 2026.

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