Helical integrity and microsolvation of transmembrane domains from Flaviviridae envelope glycoproteins
نویسندگان
چکیده
منابع مشابه
Hydrophobicity profiles in G protein-coupled receptor transmembrane helical domains.
The lack of a crystallographically derived structure for all but three G (TP [guanosine triphosphate]-binding) protein-coupled receptor (GPCRs) proteins necessitates the use of computationally derived methods to determine their structures. Computational methodologies allow a mechanistic glimpse into GPCR-ligand interactions at a molecular level to better understand the initial steps leading to ...
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15 صفحه اولDeacylation of the transmembrane domains of Sindbis virus envelope glycoproteins E1 and E2 does not affect low-pH-induced viral membrane fusion activity.
The envelope glycoproteins E1 and E2 of Sindbis virus are palmitoylated at cysteine residues within their transmembrane domains (E1 at position 430, and E2 at positions 388 and 390). Here, we investigated the in vitro membrane fusion activity of Sindbis virus variants (derived from the Toto 1101 infectious clone), in which the E1 C430 and/or E2 C388/390 residues had been substituted for alanine...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes
سال: 2011
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2011.01.004