title: The helical hydrophobic moments and surface activities of serum apolipoproteins.
abstract: The mean helical hydrophobic moments (muH) have been used to compare the amphipathic helices of several apolipoprotein classes with the helices in membrane proteins, water-soluble globular proteins and surface-active peptides. The amphipathic helices in serum apolipoproteins have similar muH and mean hydrophobicities to helices in water-soluble globular proteins. The intrinsic surface activities of proteins and peptides, as determined by surface pressure at the air/water interface, correlate with the product (muH . F) where muH is the average value of muH for all helices in the molecule, and F is the fraction of alpha-helix structure in the protein.
mesh_terms: D001053:Apolipoproteins / Q000097:blood*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008565:Membrane Proteins; D012995:Solubility; D013499:Surface Properties; D013500:Surface Tension; D014867:Water
chemical_list: D001053:Apolipoproteins; D008565:Membrane Proteins; D014867:Water