I have recently read articles about the biochemical characterisation of proteins, and see people use dimer stability, structural stability and thermal stability, I wonder what's the differences between these terms?
A protein is stable under a specific set of experimental conditions.There are various intermolecular as well as intramolecular forces that stabilize a protein. Now if there is - interaction between different monomers which result in greater stability of the resulting dimer it is called dimer stability. It has been found that greater the number of monomers greater the stability. As far a structural stability is concerned it refers to the stability of 3D structure of a given polypeptide chain. For example how hard is it to break the structure.Thermal stability refers to the resistance to denatuation/loss of conformation. Hope this help..
Hej Mohammad, Thank you for your kind answer! The terms are becoming clear to me. Just I wonder whether a greater dimer stability contributes to a greater structural stability? And whether a greater dimer stability/structural stability contributes to a greater thermal stability?
Hi there,
Dimer stability is just the consequence of Kd: the lower is the latter and the higher is the former. It has little to do with the structural stability (ie one can easily dissociate a protein dimer without affecting the structural integrity of both monomers. ITC is suitable for Kd measurement whereas DSC or Thermofluor are for structural/thermal stability.
Of course dimer will be more stable than monomer as its dissociation will require an added energy input to break up interaction forces. Further, most of the time, dimerization/oligomerization also induces some structural rearrangments resulting into a more stable conformation of the monomer.
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