ArticleJournal of molecular biology2012
Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.Biophysical journal · 2020Article
- MICA-129 Dimorphism and Soluble MICA Are Associated With the Progression of Multiple Myeloma.Frontiers in immunology · 2018Article
- A method for rapid high-throughput biophysical analysis of proteins.Scientific reports · 2017Article
- Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Journal of the Royal Society, Interface · 2015Article
- Structural origin of slow diffusion in protein folding.Science (New York, N.Y.) · 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
- The role of high-dimensional diffusive search, stabilization, and frustration in protein folding.Biophysical journal · 2014Article
- The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Journal of molecular biology · 2014Article
- Take home lessons from studies of related proteins.Current opinion in structural biology · 2013Review
- Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy.Nature communications · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The elongated three-helix-bundle spectrin domains R16 and R17 fold and unfold unusually slowly over a rough energy landscape, in contrast to the homologue R15, which folds fast over a much smoother, more typical landscape. R15 folds via a nucleation-condensation mechanism that guides the docking of the A and C-helices. However, in R16 and R17, the secondary structure forms first and the two helices must then dock in the correct register. Here, we use variants of R16 and R17 to demonstrate that substitution of just five key residues is sufficient to alter the folding mechanism and reduce the landscape roughness. We suggest that, by providing access to an alternative, faster, folding route over their landscape, R16 and R17 can circumvent their slow, frustrated wild-type folding mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.