Preferential adsorption of hydrophobic-polar model proteins on patterned surfaces.
We study the adsorption of a single hydrophobic-polar (HP) model protein under the influence of a flat but specially designed surface. A folded HP model protein is brought to the surface with a designed pattern consisting of certain attractive and repulsive sites for the different monomers (amino acids). In contrast to the deformation of a random sequence that is continuous, deformation of any protein-like sequences is unlikely and an energy gap is associated with it. The surface with a certain wavelength of pattern attracts a certain type of folded structure preferentially and the free energy of the combined system is reduced. The model presented here represents a minimal theoretical model for protein recognition.
Lee
N-K
NK
Max-Planck-Institute for Polymer Research, P.O. Box 3148, D-55021 Mainz, Germany.
Vilgis
T A
TA
D000327:Adsorption; D055592:Biophysical Phenomena; D001703:Biophysics; D015233:Models, Statistical; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D011506:Proteins