PEGylation near a patch of non-polar surface residues increases the conformational stability of the WW domain.
JOURNAL OF ORGANIC CHEMISTRY(2020)
摘要
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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关键词
conformational stability,nonpolar surface residues
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