ArticleProceedings of the National Academy of Sciences of the United States of America2010
Entropic mechanism of large fluctuation in allosteric transition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Accurate prediction of protein folding mechanisms by simple structure-based statistical mechanical models.Nature communications · 2023Article
- The Wako-Saitô-Muñoz-Eaton Model for Predicting Protein Folding and Dynamics.Molecules (Basel, Switzerland) · 2022Review
- Weakening of interaction networks with aging in tip-link protein induces hearing loss.The Biochemical journal · 2021Article
- The nicotinic acetylcholine receptor: a typical 'allosteric machine'.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- Visualizing correlated motion with HDBSCAN clustering.Protein science : a publication of the Protein Society · 2018Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Cooperativity and modularity in protein folding.Biophysics and physicobiology · 2016Review
- Characterization of protein folding by a Φ-value calculation with a statistical-mechanical model.Biophysics and physicobiology · 2016Article
- Small Molecule Targeting of Protein-Protein Interactions through Allosteric Modulation of Dynamics.Molecules (Basel, Switzerland) · 2015Review
- Allosteric Regulation of E-Cadherin Adhesion.The Journal of biological chemistry · 2015Article
- Free energy landscape of activation in a signalling protein at atomic resolution.Nature communications · 2015Article
- The role of protein dynamics in allosteric effects-introduction.Biophysical reviews · 2015Article
- Communication over the network of binary switches regulates the activation of A2A adenosine receptor.PLoS computational biology · 2015Article
- Learning To Fold Proteins Using Energy Landscape Theory.Israel journal of chemistry · 2014Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Impact of mutations on the allosteric conformational equilibrium.Journal of molecular biology · 2013Article
- Allostery in the Hsp70 chaperone proteins.Topics in current chemistry · 2013Review
- Analysis and elimination of a bias in targeted molecular dynamics simulations of conformational transitions: application to calmodulin.The journal of physical chemistry. B · 2012Article
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2 authors.
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Abstract
A statistical mechanical model of allosteric transitions in proteins is developed by extending the structure-based model of protein folding to cases of multiple native conformations. The partition function is calculated exactly within the model and the free-energy surface reflecting allostery is derived. This approach is applied to an example protein, the receiver domain of the bacterial enhancer-binding protein NtrC. The model predicts the large entropy associated with a combinatorial number of preexisting transition routes. This large entropy lowers the free-energy barrier of the allosteric transition, which explains the large structural fluctuation observed in the NMR data of NtrC. The global allosteric transformation of NtrC is explained by the shift of preexisting distribution of conformations upon phosphorylation, but the local structural adjustment around the phosphorylation site is explained by the complementary induced-fit mechanism. Structural disordering accompanied by fluctuating interactions specific to two allosteric conformations underlies a large number of routes of allosteric transition.
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