ReviewBiophysical reviews2020
Allosteric communication in molecular machines via information exchange: what can be learned from dynamical modeling.
Review in Biophysical reviews, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- TDTAC: a generalized time-dependent torsion angle correlation framework for resolving directional coordination in large biomolecular assemblies.Frontiers in molecular biosciences · 2026Article
- Dynamic claw of dengue protease unveils druggability potential with high affinity allosteric inhibitors.PNAS nexus · 2025Article
- Cooperativity in regulation of membrane protein function: phenomenological analysis of the effects of pH and phospholipids.Biophysical reviews · 2023Review
- Neural relational inference to learn long-range allosteric interactions in proteins from molecular dynamics simulations.Nature communications · 2022Article
- Distinct allosteric pathways in imidazole glycerol phosphate synthase from yeast and bacteria.Biophysical journal · 2022Article
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- Biophysical Reviews: 2020-looking back, going forward.Biophysical reviews · 2020Article
- Allostery and Epistasis: Emergent Properties of Anisotropic Networks.Entropy (Basel, Switzerland) · 2020Article
- Biophysical Reviews' national biophysical society partnership program.Biophysical reviews · 2020Article
- Probing the Structural Dynamics of theFrontiers in molecular biosciences · 2020Article
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Authors and funding
2 authors.
Funding
Abstract
Allosteric regulation is crucial for the operation of protein machines and molecular motors. A major challenge is to characterize and quantify the information exchange underlying allosteric communication between remote functional sites in a protein, and to identify the involved relevant pathways. We review applications of two topical approaches of dynamical protein modeling, a kinetic-based single-molecule stochastic model, which employs information thermodynamics to quantify allosteric interactions, and structure-based coarse-grained modeling to characterize intra-molecular couplings in terms of conformational motions and propagating mechanical strain. Both descriptions resolve the directionality of allosteric responses within a protein, emphasizing the concept of causality as the principal hallmark of protein allostery. We discuss the application of techniques from information thermodynamics to dynamic protein elastic networks and evolutionary designed model structures, and the ramifications for protein allostery.
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Registered trials
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