The contribution of α‐helices to the surface activities of proteins

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Abstract
The amphilicity of an α‐helical segment in a protein may be quantitated by calculating its mean helical hydrophobic moment (μH). For proteins whose hydrophobic interactions with interfaces are mediated by α‐helices, the surface pressures exerted at the air‐water interface correlate with the product () × F) where is the mean helical hydrophobic moment averaged over all helices in the entire molecule, and F is the fraction of α‐helix in the protein. Knowledge of μH permits a description of the contribution ofamphipathic α‐helices to the surface activities at the air‐water interface of serum apolipoproteins, surface‐seeking peptides, and globular water‐soluble proteins.