ArticleReports on progress in physics. Physical Society (Great Britain)2012
Biomolecular dynamics: order-disorder transitions and energy landscapes.
Article in Reports on progress in physics. Physical Society (Great Britain), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Mapping the energy landscape of a fold-switching protein MAD2.Protein science : a publication of the Protein Society · 2025Article
- A contact-based analysis of local energetic frustration dynamics identifies key residues enabling RfaH fold-switch.Protein science : a publication of the Protein Society · 2024Article
- Article
- Investigating the Conformational Dynamics of a Y-Family DNA Polymerase during Its Folding and Binding to DNA and a Nucleotide.JACS Au · 2022Article
- Coarse-Grained Simulations of Protein Folding: Bridging Theory and Experiments.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Dramatic Shape Changes Occur as CytochromeThe journal of physical chemistry. B · 2020Article
- POLARIS: Path of Least Action Analysis on Energy Landscapes.Journal of chemical information and modeling · 2020Article
- A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior under High Hydrostatic Pressure.The journal of physical chemistry. B · 2020Article
- The Role of Electrostatics and Folding Kinetics on the Thermostability of Homologous Cold Shock Proteins.Journal of chemical information and modeling · 2020Article
- Successes and challenges in simulating the folding of large proteins.The Journal of biological chemistry · 2020Review
- Rapid interpretation of small-angle X-ray scattering data.PLoS computational biology · 2019Article
- Structural and Dynamical Order of a Disordered Protein: Molecular Insights into Conformational Switching of PAGE4 at the Systems Level.Biomolecules · 2019Article
- Interface Residues That Drive Allosteric Transitions Also Control the Assembly of l-Lactate Dehydrogenase.The journal of physical chemistry. B · 2018Article
- Atomistic simulations indicate the functional loop-to-coiled-coil transition in influenza hemagglutinin is not downhill.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- PAGE4 and Conformational Switching: Insights from Molecular Dynamics Simulations and Implications for Prostate Cancer.Journal of molecular biology · 2018Article
- Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Royal Society open science · 2018Article
- Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.Biophysical journal · 2018Article
- On the folding of a structurally complex protein to its metastable active state.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Denaturants Alter the Flux through Multiple Pathways in the Folding of PDZ Domain.The journal of physical chemistry. B · 2018Article
- Understanding protein domain-swapping using structure-based models of protein folding.Progress in biophysics and molecular biology · 2017Review
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Authors and funding
3 authors.
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Abstract
While the energy landscape theory of protein folding is now a widely accepted view for understanding how relatively weak molecular interactions lead to rapid and cooperative protein folding, such a framework must be extended to describe the large-scale functional motions observed in molecular machines. In this review, we discuss (1) the development of the energy landscape theory of biomolecular folding, (2) recent advances toward establishing a consistent understanding of folding and function and (3) emerging themes in the functional motions of enzymes, biomolecular motors and other biomolecular machines. Recent theoretical, computational and experimental lines of investigation have provided a very dynamic picture of biomolecular motion. In contrast to earlier ideas, where molecular machines were thought to function similarly to macroscopic machines, with rigid components that move along a few degrees of freedom in a deterministic fashion, biomolecular complexes are only marginally stable. Since the stabilizing contribution of each atomic interaction is on the order of the thermal fluctuations in solution, the rigid body description of molecular function must be revisited. An emerging theme is that functional motions encompass order-disorder transitions and structural flexibility provides significant contributions to the free energy. In this review, we describe the biological importance of order-disorder transitions and discuss the statistical-mechanical foundation of theoretical approaches that can characterize such transitions.
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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.