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• W1981198140 abstract "Phosphorylated amino acids were incorporated into a designed β-hairpin peptide to study the effect on β-hairpin structure when the phosphate group is positioned to interact with a tryptophan residue on the neighboring strand. The three commonly phosphorylated residues in biological systems, serine, threonine, and tyrosine, were studied in the same β-hairpin system. It was found that phosporylation destabilizes the hairpin structure by approximately 1.0 kcal/mol, regardless of the type of phosphorylated residue. In contrast, destabilization due to glutamic acid was about 0.3 kcal/mol. Double mutant cycles and pH studies are consistent with a repulsive interaction as the source of destabilization. These findings demonstrate a novel mechanism by which phosphorylation may influence protein structure and function." @default.
• W1981198140 created "2016-06-24" @default.
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• W1981198140 creator A5034116233 @default.
• W1981198140 date "2009-09-10" @default.
• W1981198140 modified "2023-09-23" @default.
• W1981198140 title "Controlling Peptide Folding with Repulsive Interactions between Phosphorylated Amino Acids and Tryptophan" @default.
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• W1981198140 doi "https://doi.org/10.1021/ja9047575" @default.
• W1981198140 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2757742" @default.
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