Figure 2 | Scientific Reports

Figure 2

From: Docking, thermodynamics and molecular dynamics (MD) studies of a non-canonical protease inhibitor, MP-4, from Mucuna pruriens

Figure 2

Affinity and thermodynamics for trypsin analysed through SPR. SPR based thermodynamic analysis of MP-4-trypsin interaction at equilibrium. (a) Typical sensorgram for MP-4 and trypsin interaction at various concentrations. (b) KD versus temperature. (c) Natural log of KD versus inverse of temperature, slope indicate the Arrhenius values. (d) Individual contributions of enthalpy (ΔH) and entropy (TΔS) to equilibrium free energy of binding (ΔG), at temperatures ranging from 15° to 35 °C.

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