ArticleThe Journal of biological chemistry2010
The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The Conformational Plasticity Vista of PDZ Domains.Life (Basel, Switzerland) · 2020Review
- Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.Scientific reports · 2016Article
- Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus.Scientific reports · 2015Article
- Fast and accurate resonance assignment of small-to-large proteins by combining automated and manual approaches.PLoS computational biology · 2015Article
- The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.PloS one · 2014Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.Scientific reports · 2013Article
- Article
- Article
- The multiple-specificity landscape of modular peptide recognition domains.Molecular systems biology · 2011Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein domains usually fold without or with only transiently populated intermediates, possibly to avoid misfolding, which could result in amyloidogenic disease. Whether observed intermediates are productive and obligatory species on the folding reaction pathway or dispensable by-products is a matter of debate. Here, we solved the crystal structure of a small protein domain, SAP97 PDZ2 I342W C378A, and determined its folding pathway. The presence of a folding intermediate was demonstrated both by single and double-mixing kinetic experiments using urea-induced (un)folding as well as ligand-induced folding. This protein domain was found to fold via a triangular scheme, where the folding intermediate could be either on- or off-pathway, depending on the experimental conditions. Furthermore, we found that the intermediate was present at equilibrium, which is rarely seen in folding reactions of small protein domains. The folding mechanism observed here illustrates the roughness and plasticity of the protein folding energy landscape, where several routes may be employed to reach the native state. The results also reconcile the folding mechanisms of topological variants within the PDZ domain family.
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