Hydrophobic-at-interface regions in viral fusion protein ectodomains.
In this chapter we shall describe how to apply the hydrophobicity-at-interface scale, as proposed by Wimley and White [Wimley, W. C. and White, S. H. (1996) Nature Struct. Biol. 3:842-848], to the detection of amino acid sequences of viral envelope glycoproteins putatively engaged in interactions with the target membranes. In addition, a new approach will be briefly introduced to infer the bilayer location at equilibrium of membrane-partitioning sequences. The use of these new procedures may be important in describing the molecular mechanism leading to the formation of a fusion pore by viral glycoproteins.
Nieva
J L
JL
Unidad de Biofísica (CSIC-UPV/EHU) and Departamento de Bioquímica, Universidad del País Vasco, Bilbao, Spain. GBPNIESJ@lg.ehu.es
Suárez
T
T
D000595:Amino Acid Sequence; D008561:Membrane Fusion / Q000502:physiology*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000502:physiology
D014760:Viral Fusion Proteins