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

Charlotte Dodson; Eyal Arbely

doi:10.1016/j.febslet.2015.06.002

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

Charlotte Dodson, Eyal Arbely

Department of Life Sciences

MRC Centre for Protein Engineering

Research output: Contribution to journal › Article › peer-review

7 Citations (SciVal)

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.

Original language	English
Pages (from-to)	1740-1747
Number of pages	8
Journal	FEBS Letters
Volume	589
Issue number	15
DOIs	https://doi.org/10.1016/j.febslet.2015.06.002
Publication status	Published - 11 Jun 2015

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10.1016/j.febslet.2015.06.002Licence: CC BY

Using single molecule spectroscopy to inform drug discovery in protein kinases
Dodson, C. (PI)
1/12/13 → 30/11/16
Project: Project at a former HEI

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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. ",

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

Abstract

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Projects

Using single molecule spectroscopy to inform drug discovery in protein kinases

Cite this