Ontology highlight
ABSTRACT:
SUBMITTER: Dodson CA
PROVIDER: S-EPMC2851443 | biostudies-literature | 2010 May
REPOSITORIES: biostudies-literature
Dodson Charlotte A CA Ferguson Neil N Rutherford Trevor J TJ Johnson Christopher M CM Fersht Alan R AR
Protein engineering, design & selection : PEDS 20100203 5
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 t ...[more]