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- W2149460220 abstract "A disruptive interaction of phosphoserine with tryptophan in peptides that autonomously fold into a β-hairpin structure in aqueous solution was explored in a positional context within the hairpin structure. All the peptides presented here have a serine or phosphoserine directly cross strand from a tryptophan residue in the β-hairpin structure. It was observed that positioning of phosphoserine-tryptophan had a less destabilizing effect if the phosphoserine was on the C-terminus as opposed to the N-terminus. Greater destabilization was observed when the phosphoserine was positioned closer to the nucleating turn sequence rather than the termini of the hairpin. Multiple phosphorylations in a hairpin designed with two cross-strand serine-tryptophan pairs resulted in a greater decrease in hairpin formation with additional incorporations of phosphoserine. The work presented here gives further insight to destabilizing phosphoserine-tryptophan interaction within the β-hairpin model system." @default.
- W2149460220 created "2016-06-24" @default.
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- W2149460220 date "2010-01-01" @default.
- W2149460220 modified "2023-09-26" @default.
- W2149460220 title "Positional effects of phosphoserine on β-hairpin stability" @default.
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- W2149460220 doi "https://doi.org/10.1039/c0ob00202j" @default.
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