Figure 2.
Figure 2. In vitro binding of syb-2 to a syntaxin–SNAP-25 acceptor complex. (A) Fluorescence anisotropy measurements of labeled syb-2 mutants and WT protein binding to the ΔN complex. Comparison of two N-terminal mutants (LATA and VAVA) with WT syb-2 (control) and a C-terminal mutant (L84A) is shown. An N-terminally truncated syb-2 (Δ32–35, deletion of aa 32–35) displays greatly decreased binding kinetics (note the axis break on the abscissa; 100 nM synaptobrevin was added to 500 nM ΔN complex). (B) A plot of the observed binding rates of the synaptobrevin WT protein (control trace) and the LATA and VAVA mutants against the different concentrations (conc.) of the acceptor ΔN complex allows calculation of the association rate (slope of linear fits; values given in Biophysical characterization of mutants).

In vitro binding of syb-2 to a syntaxin–SNAP-25 acceptor complex. (A) Fluorescence anisotropy measurements of labeled syb-2 mutants and WT protein binding to the ΔN complex. Comparison of two N-terminal mutants (LATA and VAVA) with WT syb-2 (control) and a C-terminal mutant (L84A) is shown. An N-terminally truncated syb-2 (Δ32–35, deletion of aa 32–35) displays greatly decreased binding kinetics (note the axis break on the abscissa; 100 nM synaptobrevin was added to 500 nM ΔN complex). (B) A plot of the observed binding rates of the synaptobrevin WT protein (control trace) and the LATA and VAVA mutants against the different concentrations (conc.) of the acceptor ΔN complex allows calculation of the association rate (slope of linear fits; values given in Biophysical characterization of mutants).

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