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• W2029122944 endingPage "273" @default.
• W2029122944 startingPage "267" @default.
• W2029122944 abstract "The complete amino-acid sequence of viral fusion proteins has been analyzed by the Eisenberg procedure. The region surrounding the cleavage site contains a highly hydrophilic region immediately followed by a membrane-like region. Since the effective cleavage between these two domains seems required to expose the fusogenic domain (located at the N-terminal sequence of the transmembrane like region) which is assumed to interact with the lipid membrane of the host cell, we have focused our analysis on the conformation and mode of insertion of this membrane-like domain in a lipid monolayer. It was inserted as an alpha-helical structure into a dipalmitoylphosphatidylcholine (DPPC) monolayer and its orientation at the lipid/water interface was determined using a theoretical analysis procedure allowing the assembly of membrane components. For each viral protein sequence these N-terminal helical segments oriented obliquely with respect to the lipid/water interface. This rather unusual orientation is envisaged as a prerequisite to membrane destabilization and fusogenic activity." @default.
• W2029122944 created "2016-06-24" @default.
• W2029122944 creator A5023247580 @default.
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• W2029122944 creator A5050533193 @default.
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• W2029122944 date "1990-11-01" @default.
• W2029122944 modified "2023-10-15" @default.
• W2029122944 title "Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins" @default.
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• W2029122944 doi "https://doi.org/10.1016/0005-2736(90)90163-i" @default.
• W2029122944 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2245211" @default.
• W2029122944 hasPublicationYear "1990" @default.
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