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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions

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On the link between conformational changes, ligand binding and heat capacity.

S Vega¹, O Abian², A Velazquez-Campoy³

¹Institute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, Zaragoza, Spain.

Biochimica Et Biophysica Acta

|October 18, 2015

Summary

Protein conformational changes drive ligand binding regulation and are linked to heat capacity changes. Isothermal Titration Calorimetry (ITC) reveals these energetics, reconciling models of protein-ligand interactions.

Keywords:

Allostery Conformational change Conformational selection and induced fit Heat capacity change Isothermal titration calorimetry Ligand binding

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Area of Science:

Biochemistry
Structural Biology
Protein Dynamics

Background:

Ligand binding induces conformational changes, fundamental to protein regulation, allostery, and cooperativity.
These rearrangements are intrinsically linked to changes in heat capacity.
Isothermal Titration Calorimetry (ITC) is crucial for simultaneously measuring binding affinity, enthalpy, and heat capacity changes.

Purpose of the Study:

To address the controversy between "conformational selection" and "induced fit" models in ligand binding.
To investigate the temperature dependence of binding heat capacities in relation to conformational changes.
To reconcile different models of protein-ligand interactions, including those involving intrinsically disordered proteins.

Main Methods:

Utilizing Isothermal Titration Calorimetry (ITC) to assess conformational changes during ligand binding.
Analyzing binding energetics, including heat capacity changes.
Developing a unified model for "conformational selection" and "induced fit" scenarios.

Main Results:

Conformational equilibrium significantly contributes to binding heat capacity changes.
A unified model can explain both "conformational selection" and "induced fit" mechanisms.
Temperature-independent binding heat capacity does not preclude conformational changes.

Conclusions:

Ligand binding-induced conformational changes are a primary driver of heat capacity changes.
ITC provides critical insights into the energetics of these conformational rearrangements.
Understanding these coupled equilibria explains the dependence of binding parameters on environmental factors like temperature, pH, and ionic strength.