Binding Energetics Of The Inhibitor Cystatin To The Cysteine Proteinase Actinidin

Title: Binding Energetics Of The Inhibitor Cystatin To The Cysteine Proteinase Actinidin

Volume: 10 Issue: 2

Author(s): Maricela Neria-Rios, Jaqueline Padilla-Zuniga, Enrique Garcia-Hernandez, Salvador R. Tello-Solis and Rafael A. Zubillaga

Affiliation:

Keywords: protease-inhibitor complex, energetics, surface area models, fluorescence

Abstract: The binding energetics of actinidin to chicken cystatin was determined from fluorometric titrations at different temperatures. It is shown that the association of actinidin with cystatin is both enthalpically and entropically driven, with a negative change in the heat capacity. The molecular basis of these contributions are analyzed within the framework of surface-area models, using a 3D model of the actinidin-cystatin complex, which was obtained using the x-ray structure of the homologous complex papain-stefin B as template.

Cite this article as:

Neria-Rios Maricela, Padilla-Zuniga Jaqueline, Garcia-Hernandez Enrique, Tello-Solis R. Salvador and Zubillaga A. Rafael, Binding Energetics Of The Inhibitor Cystatin To The Cysteine Proteinase Actinidin, Protein & Peptide Letters 2003; 10 (2) . https://dx.doi.org/10.2174/0929866033479121