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Differential scanning fluorimetry of apo, autolysis resistant HIV PR in the presence and absence of fragments showing that 1F1 and 1F1-N stabilize the protease in solution, consistent with binding in the site observed in crystal structures and flap closure. (a) The presence of 5 mM 1F1 and 1F1-N increases the melting temperature of protease, as indicated by shifts in the DSF curves. (b) 1F1 and 1F1-N stabilize protease in a dose-dependent manner.
