A short overview of the experimental methods currently used to follow adsorption kinetics is given in the literature (Kurrat et al. 1994). In this section, we will focus on biophysical methods that reveal the structural changes upon adsorption approaching the molecular scale. Then we will present methods that allow combined kinetics and structural data. Finally, we will detail methods that provide information about the distribution, orientation and solvation of the adsorbed proteins.
No experimental means of direct determination of protein structure are currently available at an atomistic scale when the protein is in contact with a solid surface. However, much progress has been made to gain structural insight at various aqueous-solid interfaces. In general, the biophysical methods allowing the determination of protein structure fall into two categories: one allowing high-resolution structural characterisation such as x-ray crystallography, neutron diffraction and NMR spectroscopy, and the second providing the extent of secondary structure or information on the tertiary structure using FTIR or CD techniques.
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