Oligo(dT)
E-DNA sensors distinguish between cooperative binding
of full-length g32p and noncooperative binding of the core domain
(*III) fragment. Sensors modified with (dT)7, (dT)14, (dT)21, and (dT)80 DNA probes are
utilized to differentiate between cooperative and noncooperative binding,
with the full-length g32p and truncated core domain (*III) protein
used as targets. At high ionic strength, the full-length g32p cooperatively
binds single-strand DNA in a probe-length-dependent manner (black
lines), while the *III protein binds tightly and noncooperatively
to DNA (gray lines). As seen in the binding curves, the full-length
g32p generally exhibits weaker DNA–protein binding interactions
relative to *III protein, which is characteristic of cooperativity
between protein molecules. Except in the plots showing binding to
(dT)7, which is fit to the Langmuir expression, lines are
drawn to guide the reader’s eye.