F protein-F protein interaction within the XXXX identified by native bonding or chemical cross-linking.

@entity11750 @entity6000 @entity3208 @entity7686 @entity63751 @entity2975 @entity1520 @entity6072
The spatial arrangement of the F protein spike in the @entity7686 was studied after purifying the protein and reconstituting it in lipid vesicles (Sechoy, O., Philippot, J. R., and Bienvenue, A. (1986) Biochim. Biophys. Acta 857, 1-12). The different components of the F protein spikes were analyzed by @entity3208 - @entity2975 gel electrophoresis under various conditions of treatment, i.e. at different temperatures and @entity3208 concentrations, using different detergents for F protein solubilization (Triton X-100 and @entity6072 ), by fast protein liquid chromatography analysis, and by chemical cross-linking between subunits with bifunctional agents such as @entity63751 and @entity11750 . The F protein spike appeared to be a structurally stable complex, composed of a noncovalent association of four homooligomers, each consisting of two peptides, F1 and F2, linked by a @entity1520 bond. @entity6072 and @entity6000 solubilized the F protein, preserving the tetramer, which is probably the native form. Using chemical cross-linking, a covalent bond was formed between two monomers. We hypothesize that the tetrameric form of the F protein in its native form (spike) consists of two identical dimers that can be chemically cross-linked in a stable complex.
