ArticleProtein engineering, design & selection : PEDS2010
Engineering a two-helix bundle protein for folding studies.
Article in Protein engineering, design & selection : PEDS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Structure specific DNA recognition by the SLX1-SLX4 endonuclease complex.Nucleic acids research · 2021Article
- Protein folding of the SAP domain, a naturally occurring two-helix bundle.FEBS letters · 2015Article
- Assisted peptide folding by surface pattern recognition.Biophysical journal · 2011Article
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Authors and funding
5 authors.
Funding
Abstract
The SAP domain from the Saccharomyces cerevisiae THO1 protein contains a hydrophobic core and just two alpha-helices. It could provide a system for studying protein folding that bridges the gap between studies on isolated helices and those on larger protein domains. We have engineered the SAP domain for protein folding studies by inserting a tryptophan residue into the hydrophobic core (L31W) and solved its structure. The helical regions had a backbone root mean-squared deviation of 0.9 A from those of wild type. The mutation L31W destabilised wild type by 0.8 +/- 0.1 kcal mol(-1). The mutant folded in a reversible, apparent two-state manner with a microscopic folding rate constant of around 3700 s(-1) and is suitable for extended studies of folding.
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