Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Engineering a two-helix bundle protein for folding studies.,Dodson CA, Ferguson N, Rutherford TJ, Johnson CM, Fersht AR Protein Eng Des Sel. 2010 May;23(5):357-64. Epub 2010 Feb 3. PMID:20130106[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dodson CA, Ferguson N, Rutherford TJ, Johnson CM, Fersht AR. Engineering a two-helix bundle protein for folding studies. Protein Eng Des Sel. 2010 May;23(5):357-64. Epub 2010 Feb 3. PMID:20130106 doi:10.1093/protein/gzp080
