Effect of Surfactant Hydrophobicity on the Pathway for Unfolding of Ubiquitin
Access StatusFull text of the requested work is not available in DASH at this time ("dark deposit"). For more information on dark deposits, see our FAQ.
Shaw, Bryan F.
Schneider, Grégory F.
MetadataShow full item record
CitationShaw, 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.
AbstractThis 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.
Citable link to this pagehttp://nrs.harvard.edu/urn-3:HUL.InstRepos:33490461
- FAS Scholarly Articles