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PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW Domain
Steven R E Draper1, Dallin S Ashton1, Benjamin M Conover1
1Department of Chemistry and Biochemistry , Brigham Young University , Provo , Utah 84602 , United States.
Abstract:
Many proteins have one or more surface-exposed patches of nonpolar residues; our observations here suggest that PEGylation near such locations might be a useful strategy for increasing protein conformational stability. Specifically, we show that conjugating a PEG-azide to a propargyloxyphenylalanine via the copper(I)-catalyzed azide-alkyne cycloaddition can increase the conformational stability of the WW domain due to a favorable synergistic effect that depends on the hydrophobicity of a nearby patch of nonpolar surface residues.
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