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

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 extensive...

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Detalles Bibliográficos
Autores principales: Dodson, Charlotte A., Arbely, Eyal
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4509717/
https://www.ncbi.nlm.nih.gov/pubmed/26073259
http://dx.doi.org/10.1016/j.febslet.2015.06.002
Descripción
Sumario: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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