ArticleBiophysical journal2006
Structural comparison of the two alternative transition states for folding of TI I27.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Solution NMR study of the titin I-band IgI domain I82 shows unusual conformational dynamics.Journal of biomolecular NMR · 2026Article
- Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding.Protein engineering, design & selection : PEDS · 2011Article
- The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.Journal of molecular biology · 2009Article
- Identifying critical residues in protein folding: Insights from phi-value and P(fold) analysis.The Journal of chemical physics · 2008Article
- Capillarity-like growth of protein folding nuclei.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A simple model of backbone flexibility improves modeling of side-chain conformational variability.Journal of molecular biology · 2008Article
- Roles of beta-turns in protein folding: from peptide models to protein engineering.Biopolymers · 2008Review
- Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' {Phi}-values.Protein engineering, design & selection : PEDS · 2008Article
- Combining experiment and simulation in protein folding: closing the gap for small model systems.Current opinion in structural biology · 2008Review
- Temperature-dependent folding pathways of Pin1 WW domain: an all-atom molecular dynamics simulation of a Gō model.Biophysical journal · 2007Article
- Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.Biophysical journal · 2007Article
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Authors and funding
5 authors.
Funding
Abstract
TI I27, a beta-sandwich domain from the human muscle protein titin, has been shown to fold via two alternative pathways, which correspond to a change in the folding mechanism. Under physiological conditions, TI I27 folds by a classical nucleation-condensation mechanism (diffuse transition state), whereas at extreme conditions of temperature and denaturant it switches to having a polarized transition state. We have used experimental Phi-values as restraints in ensemble-averaged molecular dynamics simulations to determine the ensembles of structures representing the two transition states. The comparison of these ensembles indicates that when native interactions are substantially weakened, a protein may still be able to fold if it can access an alternative transition state characterized by a much larger entropic contribution. Analysis of the probability distribution of Phi-values derived from ensemble averaged simulations, enables us to identify residues that form contacts in some members of the ensemble but not in others illustrating that many interactions present in transition states are not strictly required for the successful completion of the folding process.
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