| dc.description.abstract | This research is about the protein solid surface interactions which is a very complex
phenomenon. The objective of our work is to determine the surface rate coverage occupied by
the protein by native and unfolded states where the free available space plays a key factor.
Using two different kinetics models, with and without free available space during the
unfolding process, and solving them numerically using the Runge-Kutta 4-5 order method is
the most important for us to obtain our objective. The findings strongly illustrate the effect of
the available space at the surface on the adsorption of proteins in its both states. Another
important point is to get the equilibrium between the two states which is affected by the
adsorption, desorption, transformation rates constants plus the concentration of protein in the
solution. | en_US |