Reference: Dodson CA and Arbely E (2015) Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Lett 589(15):1740-7

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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.

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Journal Article | Research Support, Non-U.S. Gov't
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Dodson CA, Arbely E
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