ArticleProceedings of the National Academy of Sciences of the United States of America2006
Multiple routes lead to the native state in the energy landscape of the beta-trefoil family.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it.
- How soluble misfolded proteins bypass chaperones at the molecular level.Nature communications · 2023Pooled it
- Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kinetics.Science advances · 2025Article
- Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein.Biophysical journal · 2023Article
- Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.Frontiers in molecular biosciences · 2023Article
- A Method for Assessing the Robustness of Protein Structures by Randomizing Packing Interactions.Frontiers in molecular biosciences · 2022Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Measuring the average shape of transition paths during the folding of a single biological molecule.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Folding pathway of a multidomain protein depends on its topology of domain connectivity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Altered backbone and side-chain interactions result in route heterogeneity during the folding of interleukin-1β (IL-1β).Biophysical journal · 2013Article
- Early folding events protect aggregation-prone regions of a β-rich protein.Structure (London, England : 1993) · 2013Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Allosteric control in a metalloprotein dramatically alters function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Understanding the folding-function tradeoff in proteins.PloS one · 2013Article
- Biomolecular dynamics: order-disorder transitions and energy landscapes.Reports on progress in physics. Physical Society (Great Britain) · 2012Article
- Bivalent carbohydrate binding is required for biological activity of Clitocybe nebularis lectin (CNL), the N,N'-diacetyllactosediamine (GalNAcβ1-4GlcNAc, LacdiNAc)-specific lectin from basidiomycete C. nebularis.The Journal of biological chemistry · 2012Article
- Optimizing ring assembly reveals the strength of weak interactions.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- β-Bulge triggers route-switching on the functional landscape of interleukin-1β.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Folding circular permutants of IL-1β: route selection driven by functional frustration.PloS one · 2012Article
- The plasticity of the β-trefoil fold constitutes an evolutionary platform for protease inhibition.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
In general, the energy landscapes of real proteins are sufficiently well designed that the depths of local energetic minima are small compared with the global bias of the native state. Because of the funneled nature of energy landscapes, models that lack energetic frustration have been able to capture the main structural features of the transition states and intermediates found in experimental studies of both small and large proteins. In this study we ask: Are the experimental differences in folding mechanisms among members of a particular structural family due to local topological constraints that deviate from the tertiary fold common to the family? The beta-trefoil structural family members IL-1beta, hisactophilin, and acidic/basic FGFs were chosen to address this question. It has been observed that the topological landscape of the beta-trefoils allows for the population of diverse, geometrically disconnected routes that provide energetically similar but structurally distinct ways for this family to fold. Small changes in topology or energetics can alter the preferred route. Taken together, these results indicate that the global fold of the beta-trefoil family determines the energy landscape but that the routes accessed on that landscape might differ as a result of functional requirements of the individual family members.
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