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
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author Dodson, Charlotte A.
Arbely, Eyal
author_facet Dodson, Charlotte A.
Arbely, Eyal
author_sort Dodson, Charlotte A.
collection PubMed
description 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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spelling pubmed-45097172015-08-01 Protein folding of the SAP domain, a naturally occurring two-helix bundle Dodson, Charlotte A. Arbely, Eyal FEBS Lett Article 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. Elsevier Science B.V 2015-07-08 /pmc/articles/PMC4509717/ /pubmed/26073259 http://dx.doi.org/10.1016/j.febslet.2015.06.002 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Dodson, Charlotte A.
Arbely, Eyal
Protein folding of the SAP domain, a naturally occurring two-helix bundle
title Protein folding of the SAP domain, a naturally occurring two-helix bundle
title_full Protein folding of the SAP domain, a naturally occurring two-helix bundle
title_fullStr Protein folding of the SAP domain, a naturally occurring two-helix bundle
title_full_unstemmed Protein folding of the SAP domain, a naturally occurring two-helix bundle
title_short Protein folding of the SAP domain, a naturally occurring two-helix bundle
title_sort protein folding of the sap domain, a naturally occurring two-helix bundle
topic Article
url 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
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