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The structural stability and the conformational dynamics of animal diseases in porcine odorant-binding protein (pOBP) was investigated by employing steady-state and time-resolved fluorescence spectroscopy as well as circular dichroism experiments. The difference in free energy between native and unfolded states of pOBP in the absence of GdnHCl indicate that the protein molecule is very stable to the denaturing action of GdnHCl.

The effect of the pressure on the structure and stability of the D-galactose/D-glucose binding protein from Escherichia coli in the absence (GGBP) and in the presence (GGBP/Glc) of glucose is studied by Fourier transform infrared (FT-IR) spectroscopy and molecular dynamic (MD) simulations. FT-IR spectroscopy experiments showed that the protein [beta]-structures are more resistance than [alpha]-helices structures to pressure value increases.

The conformational changes of the Escherichia coli glutamine-binding protein (GlnBP) induced by GdnBP and the effect of the binding of glutamine (Gln) on these processes is studied. The use of the parametric presentation of fluorescence data showed that both GlnBP unfolding and GlnBP-Gn unfolding are three-step processes (N->I(sub 1)->I9sub 2)->U), though in the case of the GlnBP-Gln complex these stages essentially overlap.