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Phosphorylation stabilizes the N-termini of α-helices

✍ Scribed by Jason L. Smart; J. Andrew McCammon

Publisher
Wiley (John Wiley & Sons)
Year
1999
Tongue
English
Weight
297 KB
Volume
49
Category
Article
ISSN
0006-3525

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✦ Synopsis

The role of phosphorylation in stabilizing the N-termini of ␣-helices is examined using computer simulations of model peptides. The models comprise either a phosphorylated or unphosphorylated serine at the helix N-terminus, followed by nine alanines. Monte Carlo/stochastic Dynamics simulations were performed on the model helices. The simulations revealed a distinct stabilization of the helical conformation at the N-terminus after phosphorylation. The stabilization was attributable to favorable electrostatic interactions between the phosphate and the helix backbone. However, direct helix capping by the phosphorylated sidechain was not observed. The results of the calculations are consistent with experimental evidence on the stabilization of helices by phosphates and other anions.

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