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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. ?-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.

SUBMITTER: Dodson CA

PROVIDER: S-EPMC4509717 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature

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

Dodson Charlotte A CA Arbely Eyal E

FEBS letters 20150611 15

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 ...[more]

PMID: 26073259

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