Label-free Protein Folding studied with MicroScale Thermophoresis (MST)
MicroScale Thermophoresis (MST) was firstly applied for scrutinizing protein unfolding. In this study, a virus capsid protein was demonstrated to unfold in a three-state transition, from native to an intermediate state and finally the completely denatured protein. MST confirmed the existence of all three states that are detected by CD spectroscopy and fluorescence emission spectroscopy.
MST allows fast protein unfolding studies using only a fraction of the sample amount used in standard methods. In addition detection of states that are invisible to FES and far- UV CD spectroscopy is possible since MST is sensitive to the hydration shell of a molecule as a whole.