ArticleJournal of chemical theory and computation2019
Configurational Entropy Components and Their Contribution to Biomolecular Complex Formation.
Article in Journal of chemical theory and computation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Ensemble Effects on Hydroxide Bond Dissociation Free Energies in Polyoxovanadate Clusters.The journal of physical chemistry. A · 2026Article
- Tutorial on quantifying and sampling biomolecular ensembles with ShapeGMM.The Journal of chemical physics · 2025Article
- Tracking and Controlling Monolayer Water in Gold Nanogaps using Extreme Plasmonic Spectroscopy.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Conformational dynamics and multimodal interaction of Paxillin with the focal adhesion targeting domain.Science advances · 2025Article
- Conformational dynamics and multi-modal interaction of Paxillin with the Focal Adhesion Targeting Domain.bioRxiv : the preprint server for biology · 2025Article
- A new view of missense mutations in α-mannosidosis using molecular dynamics conformational ensembles.Protein science : a publication of the Protein Society · 2025Article
- Temporal complexity of LVV-hemorphin-7 allosterism at the angiotensin II type 1 receptor assessed using entropy-based approaches.Computational and structural biotechnology journal · 2025Article
- How pairs of insertion mutations impact protein structure: an exhaustive computational study.Bioinformatics advances · 2024Article
- Selectively tuning ionic thermopower in all-solid-state flexible polymer composites for thermal sensing.Nature communications · 2022Article
- X-Entropy: A Parallelized Kernel Density Estimator with Automated Bandwidth Selection to Calculate Entropy.Journal of chemical information and modeling · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Configurational entropy change is a central constituent of the free energy change in noncovalent interactions between biomolecules. Due to both experimental and computational limitations, however, the impact of individual contributions to configurational entropy change remains underexplored. Here, we develop a novel, fully analytical framework to dissect the configurational entropy change of binding into contributions coming from molecular internal and external degrees of freedom. Importantly, this framework accounts for all coupled and uncoupled contributions in the absence of an external field. We employ our parallel implementation of the maximum information spanning tree algorithm to provide a comprehensive numerical analysis of the importance of the individual contributions to configurational entropy change on an extensive set of molecular dynamics simulations of protein binding processes. Contrary to commonly accepted assumptions, we show that different coupling terms contribute significantly to the overall configurational entropy change. Finally, while the magnitude of individual terms may be largely unpredictable a priori, the total configurational entropy change can be well approximated by rescaling the sum of uncoupled contributions from internal degrees of freedom only, providing support for NMR-based approaches for configurational entropy change estimation.
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