title: Protein folding of the SAP domain, a naturally occurring two-helix bundle.
abstract: The SAP domain from the Saccharomyces cerevisiae Tho1 protein is comprised of just two helices and a hydrophobic core and is one of the smallest proteins whose folding has been characterised. Φ-value analysis revealed that Tho1 SAP folds through a transition state where helix 1 is the most extensively formed element of secondary structure and flickering native-like core contacts from Leu35 are also present. The contacts that contribute most to native state stability of Tho1 SAP are not formed in the transition state.
authors.affiliation: MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK; Molecular Medicine, National Heart & Lung Institute, Imperial College London, SAF Building, London SW7 2AZ, UK. Electronic address: c.dodson@imperial.ac.uk.
authors.forename: Charlotte A
authors.initials: CA
authors.lastname: Dodson
authors.affiliation: MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK.
authors.forename: Eyal
authors.initials: E
authors.lastname: Arbely
mesh_terms: D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D017510:Protein Folding; D017433:Protein Structure, Secondary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D012997:Solvents / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D012997:Solvents
keywords: Protein folding; SAP domain; Tho1; Transition state analysis; Φ-value