ArticleNature structural & molecular biology2009
The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints.
Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.Molecules (Basel, Switzerland) · 2025Article
- Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovery of an on-pathway protein folding intermediate illuminates the kinetic competition between folding and misfolding.bioRxiv : the preprint server for biology · 2024Article
- Frustraevo: a web server to localize and quantify the conservation of local energetic frustration in protein families.Nucleic acids research · 2024Article
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- A Glimpse into the Structural Properties of the Intermediate and Transition State in the Folding of Bromodomain 2 Domain 2 by Φ Value Analysis.International journal of molecular sciences · 2021Article
- Effects of Topology and Sequence in Protein Folding Linked via Conformational Fluctuations.Biophysical journal · 2020Article
- Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.The Journal of biological chemistry · 2018Article
- Folding while bound to chaperones.Current opinion in structural biology · 2018Review
- Molecular recognition and packing frustration in a helical protein.PLoS computational biology · 2017Article
- A molecular mechanism of chaperone-client recognition.Science advances · 2016Article
- Forces Driving Chaperone Action.Cell · 2016Article
- Visualizing chaperone-assisted protein folding.Nature structural & molecular biology · 2016Article
- Substrate protein folds while it is bound to the ATP-independent chaperone Spy.Nature structural & molecular biology · 2016Article
- Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.Methods (San Diego, Calif.) · 2015Article
- Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.PLoS computational biology · 2015Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- Frustration in biomolecules.Quarterly reviews of biophysics · 2014Review
- Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Conformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7.Protein science : a publication of the Protein Society · 2013Article
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5 authors.
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Abstract
Many proteins reach their native state through pathways involving the presence of folding intermediates. It is not clear whether this type of folding landscape results from insufficient evolutionary pressure to optimize folding efficiency, or arises from a conflict between functional and folding constraints. Here, using protein-engineering, ultra-rapid mixing and stopped-flow experiments combined with restrained molecular dynamics simulations, we characterize the transition state for the formation of the intermediate populated during the folding of the bacterial immunity protein, Im7, and the subsequent molecular steps leading to the native state. The results provide a comprehensive view of the folding process of this small protein. An analysis of the contributions of native and non-native interactions at different stages of folding reveals how the complexity of the folding landscape arises from concomitant evolutionary pressures for function and folding efficiency.
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