Add time:08/12/2019 Source:sciencedirect.com
In this study the pH dependence of the thermodynamic stability of tendamistat is analyzed. This small globular protein of 74 residues shows a very marked dependence of thermal stability on pH: the denaturation temperature increases from 68.9°C at pH 2.0 to 93.2°C at pH 5.0, and then decreases to 77.8°C at pH 8.0. Analysis of the data indicates that the binding of two protons is coupled to the thermal unfolding at pH values below 4.0, whereas one proton is released by the protein at pH values above 5.0. By linking the proton binding to the conformational unfolding equilibrium, a thermodynamic model, which is able to describe the dependence upon the solution pH of the denaturation Gibbs energy change for tendamistat, is developed.
We also recommend Trading Suppliers and Manufacturers of tendamistat (12-26) (cas 135307-06-1). Pls Click Website Link as below: cas 135307-06-1 suppliers
About|Contact|Cas|Product Name|Molecular|Country|Encyclopedia
Message|New Cas|MSDS|Service|Advertisement|CAS DataBase|Article Data|Manufacturers | Chemical Catalog
©2008 LookChem.com,License: ICP
NO.:Zhejiang16009103
complaints:service@lookchem.com Desktop View