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

Charlotte A. Dodson; Eyal Arbely

doi:10.1016/j.febslet.2015.06.002

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

Charlotte A. Dodson, Eyal Arbely

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

7 Scopus citations

Abstract

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
Article number	37213
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
State	Published - 3 Jul 2015
Externally published	Yes

Keywords

Protein folding
SAP domain
Tho1
Transition state analysis
Φ-value

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2015.06.002

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

abstract = "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.",

keywords = "Protein folding, SAP domain, Tho1, Transition state analysis, Φ-value",

author = "Dodson, {Charlotte A.} and Eyal Arbely",

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AU - Dodson, Charlotte A.

AU - Arbely, Eyal

PY - 2015/7/3

Y1 - 2015/7/3

N2 - 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.

AB - 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.

KW - Protein folding

KW - SAP domain

KW - Tho1

KW - Transition state analysis

KW - Φ-value

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M3 - Article

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JO - FEBS Letters

JF - FEBS Letters

IS - 15

M1 - 37213

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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