Assessing Coupled Protein Folding and Binding Through Temperature-Dependent Isothermal Titration Calorimetry

Author(s):  
Debashish Sahu ◽  
Monique Bastidas ◽  
Chad W. Lawrence ◽  
William G. Noid ◽  
Scott A. Showalter
Computation ◽  
2019 ◽  
Vol 7 (3) ◽  
pp. 46
Author(s):  
Franziska Erlekam ◽  
Sinaida Igde ◽  
Susanna Röblitz ◽  
Laura Hartmann ◽  
Marcus Weber

In addition to the conventional Isothermal Titration Calorimetry (ITC), kinetic ITC (kinITC) not only gains thermodynamic information, but also kinetic data from a biochemical binding process. Moreover, kinITC gives insights into reactions consisting of two separate kinetic steps, such as protein folding or sequential binding processes. The ITC method alone cannot deliver kinetic parameters, especially not for multivalent bindings. This paper describes how to solve the problem using kinITC and an invariant subspace projection. The algorithm is tested for multivalent systems with different valencies.


2009 ◽  
Vol 89 (3-4) ◽  
pp. 257-267 ◽  
Author(s):  
Latha-Selvi Canabady-Rochelle ◽  
Christian Sanchez ◽  
Michel Mellema ◽  
Sylvie Banon

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