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Preferential adsorption of hydrophobic-polar model proteins on patterned surfaces

MPG-Autoren
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Lee,  N. K.
MPI for Polymer Research, Max Planck Society;

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Vilgis,  Thomas A.
MPI for Polymer Research, Max Planck Society;

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Zitation

Lee, N. K., & Vilgis, T. A. (2003). Preferential adsorption of hydrophobic-polar model proteins on patterned surfaces. Physical Review E, 67(5): 050901.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000F-621E-5
Zusammenfassung
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 proteinlike 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.