The influence of the binding of methaemoproteins to latex particles with respect to protein conformation was examined using the longitudinal magnetic relaxation rates of solvent protons. The temperature dependences of the paramagnetically induced molar relaxation rates in bound metmyoglobin samples as well as their absolute values suggest an opening of the haem-pocket. The decrease of the same parameter for the immobilized methaemoglobin points to a smaller haem-pocket accessibility with respect to that in the solution. The changes of the haem-pocket structure found for both methaemoproteins support the idea that proteins change their conformation by their binding to the solid surface, although in opposite ways.
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Colloid and Surface Chemistry