Positional effects of phosphoserine on β-hairpin stability.
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.
Riemen
Alexander J
AJ
Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.
Waters
Marcey L
ML
D010455:Peptides / Q000737:chemistry*; D010768:Phosphoserine / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D010455:Peptides; D010768:Phosphoserine