ArticleBiophysical journal2016
Structure-Based Prediction of Protein-Folding Transition Paths.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Exploring force-driven stochastic folding dynamics in mechano-responsive proteins and implications in phenotypic variation.Nature communications · 2025Article
- Recent Advances in Protein Folding Pathway Prediction through Computational Methods.Current medicinal chemistry · 2024Review
- Einstein Model of a Graph to Characterize Protein Folded/Unfolded States.Molecules (Basel, Switzerland) · 2023Article
- Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain.Biophysical journal · 2023Article
- Multi-layer sequential network analysis improves protein 3D structural classification.Proteins · 2022Article
- Slowest-first protein translation scheme: Structural asymmetry and co-translational folding.Biophysical journal · 2021Article
- Article
- Validation of DBFOLD: An efficient algorithm for computing folding pathways of complex proteins.PLoS computational biology · 2020Article
- Effects of Single Mutations on Protein Stability Are Gaussian Distributed.Biophysical journal · 2020Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Accurate Protein-Folding Transition-Path Statistics from a Simple Free-Energy Landscape.The journal of physical chemistry. B · 2018Article
- Protein folding transition path times from single molecule FRET.Current opinion in structural biology · 2018Review
- Article
- Evidence of evolutionary selection for cotranslational folding.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Folding Proteins One Loop at a Time.Biophysical journal · 2016Article
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2 authors.
Funding
Abstract
We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are formed between a specific set of substructures, after which folding proceeds downhill in free energy. This approach suggests a natural resolution for distinguishing parallel folding pathways and provides a simple means to predict the rate-limiting step in a folding reaction. Our theory identifies a common folding mechanism for proteins with diverse native structures and establishes general principles for the self-assembly of polymers with specific interactions.
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