Internal protein dynamics upon ligand binding.

Molecular dynamics are of vital importance for the biological function of proteins. The proposed system of biotin and streptavidin has a stoichiometry of 4 biotin per protein. The thermal stability of streptavidin has been shown to be affected by the ratio of biotin to streptavidin.[1] Previous experiments have shown that internal dynamics change upon saturation of streptavidin with biotin. Therefore, measurements at different biotin streptavidin ratios are of interest. A Fourier transformation of the data allows for the extension of the dynamic range and thus overlaps with the timescale analysed in the proposed IRIS experiment. The proposed hypothesis is that even the binding of one biotin to streptavidin modifies the whole internal dynamics1. M.Gonzales et al. 1999, Biomolecular Engineering, 16 67-72