AI Article Synopsis
- The binding of actinidin to chicken cystatin was studied using fluorometric titrations at various temperatures, revealing that the interaction is driven by both enthalpy and entropy.
- These findings indicate a negative change in heat capacity during the binding process.
- The analysis involved surface-area models and utilized a 3D structural model of the actinidin-cystatin complex based on the x-ray structure of the similar papain-stefin B complex.
Article 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.
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| http://dx.doi.org/10.2174/0929866033479121 | DOI Listing |
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