Protein folding of the SAP domain, a naturally occurring two-helix bundle

3Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

Dodson, C. A., & Arbely, E. (2015). Protein folding of the SAP domain, a naturally occurring two-helix bundle. FEBS Letters, 589(15), 1740–1747. https://doi.org/10.1016/j.febslet.2015.06.002

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free