Plasminogen undergoes a large conformational change when it binds 6-aminohe
xanoate. Using ultraviolet absorption spectroscopy and native PAGE, we show
that hydrostatic pressure brings about the same conformational change. The
volume change for this conformational change is -33 mL.mol(-1). Binding of
ligand and hydrostatic pressure both cause the protein to open up to expos
e surfaces that had previously been buried in the interior.