Open-ITC: an alternate computational approach to analyze the isothermal titration calorimetry data of complex binding mechanisms

2011 ◽  
Vol 24 (6) ◽  
pp. 1056-1066 ◽  
Author(s):  
Janarthanan Krishnamoorthy ◽  
Smita Mohanty
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Computational Approach ◽  
Titration Calorimetry ◽  
Calorimetry Data ◽  
Binding Mechanisms

scholarly journals Prediction of self-assembly of adenosine analogues in solution: a computational approach validated by isothermal titration calorimetry

2019 ◽  
Vol 21 (8) ◽  
pp. 4258-4267 ◽  
Author(s):  
Luca Redivo ◽  
Rozalia-Maria Anastasiadi ◽  
Marco Pividori ◽  
Federico Berti ◽  
Maria Peressi ◽  
...  
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Self Assembly ◽  
Computational Approach ◽  
Titration Calorimetry ◽  
Cognitive Enhancers ◽  
Adenosine Analogues ◽  
Therapeutic Drugs

The recent discovery of the role of adenosine-analogues as neuroprotectants and cognitive enhancers has sparked interest in these molecules as new therapeutic drugs.

scholarly journals Resolving Three-State Ligand-Binding Mechanisms by Isothermal Titration Calorimetry: A Simulation Study

2017 ◽  
Author(s):  
Evgenii L. Kovrigin
Keyword(s):  
Ligand Binding ◽  
Isothermal Titration Calorimetry ◽  
Simulation Study ◽  
Titration Calorimetry ◽  
Induced Fit ◽  
State Process ◽  
Binding Mechanisms

ABSTRACTIn this paper, I theoretically analyzed ITC profiles for three-state equilibria involving ligand binding coupled to isomerization or dimerization transitions. Simulations demonstrate that the mechanisms where the free or ligand-bound protein undergoes dimerization (such that the ligand cannot bind to or dissociate from the dimer) produce very distinctive titration profiles. In contrast, profiles of the pre-existing equilibrium or induced-fit models cannot be distinguished from a simple two-state process, requiring data from additional techniques to positively identify these mechanisms.

scholarly journals pytc: Open-Source Python Software for Global Analyses of Isothermal Titration Calorimetry Data

Biochemistry ◽  
2018 ◽  
Vol 57 (18) ◽  
pp. 2578-2583 ◽  
Author(s):  
Hiranmayi Duvvuri ◽  
Lucas C. Wheeler ◽  
Michael J. Harms
Keyword(s):  
Open Source ◽  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry ◽  
Calorimetry Data

scholarly journals Titration Calorimetry Standards and the Precision of Isothermal Titration Calorimetry Data

2009 ◽  
Vol 10 (6) ◽  
pp. 2752-2762 ◽  
Author(s):  
Lina Baranauskienė ◽  
Vilma Petrikaitė ◽  
Jurgita Matulienė ◽  
Daumantas Matulis
Keyword(s):  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry ◽  
Calorimetry Data

scholarly journals Re-visiting the trans insertion model for complexin clamping

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Shyam S Krishnakumar ◽  
Feng Li ◽  
Jeff Coleman ◽  
Curtis M Schauder ◽  
Daniel Kümmel ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Isothermal Titration Calorimetry ◽  
Neurotransmitter Release ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Titration Calorimetry ◽  
Nmr Study ◽  
Cross Links ◽  
Calorimetry Data

We have previously proposed that complexin cross-links multiple pre-fusion SNARE complexes via a trans interaction to function as a clamp on SNARE-mediated neurotransmitter release. A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previous interpretation of the fluorescence resonance energy transfer and isothermal titration calorimetry data on which the trans clamping model was originally based. Here we present new biochemical data that underscore the validity of our previous interpretation and the continued relevancy of the trans insertion model for complexin clamping.

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