Both differential scanning (DSC) and isothermal titration microcalorimetry (ITC) can be used to study macromolecules.  Though the heat effects of macromolecular interactions are small, highly sensitive instruments can determine the energetics and stoichiometry by detecting the heat energy changes accompanying  associations or dissociation (intra- or inter-) processes (changes in temperature at a fixed solvent condition or change in solvent condition at fixed temperature).  The increase in heat capacity of native proteins with temperature reflects an accumulation of energy upon heating the results from changes in (hydrated) protein structure and not just intensifying vibrations.  Titration calorimetry allows simulataneous determination of equilibrium constants and enthalpy changes, from which the changes in the standard Gibbs energy and entropy can be derived.
    Improvements in instrumentation have greatly advanced the use of microcalorimetry for biological samples.  For example, more stable DSC showed the native and unfolded protein heat capacities do not change in parallel with temperature (Privalov, 1988) as had been previously assumed. 

Applications:

1. Protein folding/unfolding
2. DNA/protein association
3. cyclodextrin/protein interaction
4. liposome/drug complex
5. polymer/amphiphile interaction (cmc)
   

Pros:

1. proteins do not have to be labeled or attached to a surface
   
2. DSC has a wide operational range (temp and pressure)
3. ITC very sensitive (nanomolar amounts needed)
   

Cons:

1. low sample through put (ITC)
2. lack of specificity