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. Author manuscript; available in PMC: 2014 Oct 29.
Published in final edited form as: Biochemistry. 2013 Oct 15;52(43):7678–7688. doi: 10.1021/bi400962r

Figure 6.

Figure 6

Effect of dimer stability on inhibitor binding and thermal denaturation of single-chain PR constructs, ScPR (dark red) and ScPRD25N (black) in comparison with PR (orange) and PRD25N (blue) homodimers. Dashed and solid lines designate scans without inhibitor and with ~2-fold molar excess of inhibitor RPB or DRV relative to the respective proteases (as dimers). ΔTm values shown for each pair of traces show the increase in Tm of each protein upon inhibitor binding. For experimental details see Materials and Methods. Actual Tm values are given in Table 1B.