Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin

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Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin

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Title: Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin
Author: Shaw, Bryan F.; Schneider, Grégory F.; Whitesides, George M.

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Citation: Shaw, Bryan F., Grégory F. Schneider, and George M. Whitesides. 2012. “Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin.” Journal of the American Chemical Society 134 (45) (November 14): 18739–18745. doi:10.1021/ja3079863.
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Abstract: This paper describes the interaction between ubiquitin (UBI) and three sodium n-alkyl sulfates (SCnS) that have the same charge (Z = −1) but different hydrophobicity (n = 10, 12, or 14). Increasing the hydrophobicity of the n-alkyl sulfate resulted in (i) an increase in the number of distinct intermediates (that is, complexes of UBI and surfactant) that form along the pathway of unfolding, (ii) a decrease in the minimum concentrations of surfactant at which intermediates begin to form (i.e., a more negative ΔGbinding of surfactant for UBI), and (iii) an increase in the number of surfactant molecules bound to UBI in each intermediate or complex. These results demonstrate that small changes in the hydrophobicity of a surfactant can significantly alter the binding interactions with a folded or unfolded cytosolic protein.
Published Version: doi:10.1021/ja3079863
Other Sources: http://www.shawlaboratory.com/pub/15.pdf
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:33490461
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