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Protein folding of the SAP domain, a naturally occurring two-helix bundle
File(s)
Author(s)
Dodson, CA
Arbely, E
Type
Journal Article
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.
Date Issued
2015-06-11
Date Acceptance
2015-06-01
Citation
FEBS Letters, 2015, 589 (15), pp.1740-1747
URI
DOI
ISSN
1873-3468
Publisher
Elsevier
Start Page
1740
End Page
1747
Journal / Book Title
FEBS Letters
Volume
589
Issue
15
Copyright Statement
© 2015 the Author(s) This article is available under the terms of the Creative Commons Attribution License (CC BY). You may copy and distribute the article, create extracts, abstracts and new works from the article, alter and revise the article, text or data mine the article and otherwise reuse the article commercially (including reuse and/or resale of the article) without permission from Elsevier. You must give appropriate credit to the original work, together with a link to the formal publication through the relevant DOI and a link to the Creative Commons user license above. You must indicate if any changes are made but not in any way that suggests the licensor endorses you or your use of the work.
License URL
Publication Status
Published