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Essentially identical SEC3 binding behavior was observed for peptide-free and peptide-loaded DR1 (Figure 4A C).
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Interestingly, two differing types of binding behavior were observed among the three selected anticalins.
A similar behavior was observed previously for YFP-labeled protein homodimers and used to detect protein reorientation upon binding.
Noteworthy, this unexpected behavior was observed only for the BH3 domain of BAX, and may indicate a role in membrane binding specifically for this protein (see below).
The opposite behavior was observed for aw.
The behavior was observed in a laboratory.
In Figure2a, a kink behavior was observed.
Similar behavior was observed for PEG volume.
A dichotomy between diurnal and nocturnal diving behavior was observed.
Similar behavior was observed with RecA.
This behavior was observed for N = 5 gels.
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