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• W2007334365 abstract "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." @default.
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• W2007334365 date "2003-05-28" @default.
• W2007334365 modified "2023-09-25" @default.
• W2007334365 title "Preferential adsorption of hydrophobic-polar model proteins on patterned surfaces" @default.
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• W2007334365 doi "https://doi.org/10.1103/physreve.67.050901" @default.
• W2007334365 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12786127" @default.
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