Figure 4From: Structural basis of RGD-hirudin binding to thrombin: Tyr3 and five C-terminal residues are crucial for inhibiting thrombin activitySPR measurement of the interactions of RGD-hirudin and mutant variants with thrombin. (A-G) KD values. BIAcore analysis showed that the binding affinity of thrombin and wild-type RGD-hirudin was slightly stronger than those of the six mutants. (H) Affinity curves (with proteins at 100nM) demonstrated that the binding affinities of thrombin and the six mutants were weaker than that of RGD-hirudin.Back to article page