| Literature DB >> 6652103 |
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.Entities:
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Year: 1983 PMID: 6652103 DOI: 10.1016/0005-2760(83)90165-0
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002