The long and the short of it: Just by changing the polarity of the solvent the highly folded heptapeptide Ac-[Aib-L-(αMe)Val-Aib]2-L-His-NH2 converts from an α into a 310 helix (see picture). The equilibrium constant between the two conformations correlates with the empirical solvent polarity parameter Eequation image. Molecular dynamics calculations show that the peptide elongates (310 helix) or shortens (α helix) on switching from one conformation to the other.
Quantitative correlation of solvent polarity with the alpha-/3(10)-helix equilibrium: A heptapeptide behaves as a solvent-driven molecular spring
PENGO, PAOLO;PASQUATO, LUCIA;MORO, STEFANO;BRIGO, ALESSANDRO;SCRIMIN, PAOLO MARIA
2003
Abstract
The long and the short of it: Just by changing the polarity of the solvent the highly folded heptapeptide Ac-[Aib-L-(αMe)Val-Aib]2-L-His-NH2 converts from an α into a 310 helix (see picture). The equilibrium constant between the two conformations correlates with the empirical solvent polarity parameter Eequation image. Molecular dynamics calculations show that the peptide elongates (310 helix) or shortens (α helix) on switching from one conformation to the other.
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