ReviewNature chemical biology2025
Advances in uncovering the mechanisms of macromolecular conformational entropy.
Review in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed.
- Conformational Dynamics of Viral Protease Precursors in Maturation, Inhibition, and Drug-Resistance Development.Viruses · 2026Review
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- From possibility to precision in macromolecular ensemble prediction.Nature methods · 2026Article
- Thermodynamically guided kilogram-scale precipitation of copper iodide clusters for efficient solution-processed light-emitting diodes.Science advances · 2026Article
- Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration.Science (New York, N.Y.) · 2026Article
- Artificial allosteric protein switches with machine-learning-designed receptors.Nature biotechnology · 2026Article
- The genetic architecture of an allosteric hormone receptor.Nature communications · 2026Article
- A novel biomacromolecule-predominated hybrid unit: from design, characterization to application.National science review · 2026Article
- The Power of Protein Dynamics in Binding and Allostery.Biochemistry · 2026Review
- Protein structure and coupled solvent dynamics in α-synuclein fibrils under controlled confinement.Biophysical journal · 2026Article
- PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation.Nature communications · 2026Article
- An inter-subunit path is required for entropically-driven and negatively cooperative binding of cyclic nucleotides in the HCN2 channel.Communications biology · 2026Article
- Biological Systems Depend on Communication Over Distances: A Review of the Fundamental Mechanisms, Associated challenges, and the Potential Effect of the Constrained Disorder Principle.Acta biotheoretica · 2026Review
- Crystallographic Ensembles Reveal the Structural Basis of Binding Entropy in SARS-CoV2 Macrodomain.bioRxiv : the preprint server for biology · 2025Article
- Reaching the full potential of cryo-EM reconstructions with molecular dynamics simulations at 310 K: Actin filaments as an example.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Allosteric binding cooperativity in kinases signaling, signalopathies, and drug development.Current opinion in structural biology · 2025Review
- Sparse networks of conformational fluctuations communicate signals within proteins.bioRxiv : the preprint server for biology · 2025Article
- Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release.Nature communications · 2025Article
- The Arch from the Stones: Understanding Protein Folding Energy Landscapes via Bioinspired Collective Variables.The journal of physical chemistry letters · 2025Article
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
During protein folding, proteins transition from a disordered polymer into a globular structure, markedly decreasing their conformational degrees of freedom, leading to a substantial reduction in entropy. Nonetheless, folded proteins retain substantial entropy as they fluctuate between the conformations that make up their native state. This residual entropy contributes to crucial functions like binding and catalysis, supported by growing evidence primarily from NMR and simulation studies. Here, we propose three major ways that macromolecules use conformational entropy to perform their functions; first, prepaying entropic cost through ordering of the ground state; second, spatially redistributing entropy, in which a decrease in entropy in one area is reciprocated by an increase in entropy elsewhere; third, populating catalytically competent ensembles, in which conformational entropy within the enzymatic scaffold aids in lowering transition state barriers. We also provide our perspective on how solving the current challenge of structurally defining the ensembles encoding conformational entropy will lead to new possibilities for controlling binding, catalysis and allostery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.