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          Institute: MPI für Polymerforschung     Collection: MPI Polymerforschung     Display Documents



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ID: 56205.0, MPI für Polymerforschung / MPI Polymerforschung
Preferential adsorption of hydrophobic-polar model proteins on patterned surfaces
Authors:Lee, N. K.; Vilgis, Thomas A.
Language:English
Date of Publication (YYYY-MM-DD):2003-05
Title of Journal:Physical Review E
Journal Abbrev.:Phys. Rev. E
Volume:67
Issue / Number:5
Sequence Number of Article:050901
Review Status:not specified
Audience:Not Specified
Abstract / Description: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.
Comment of the Author/Creator:Date: 2003, MAY
External Publication Status:published
Document Type:Article
Affiliations:MPI für Polymerforschung
Identifiers:ISI:000183482200009 [ID No:1]
ISSN:1063-651X [ID No:2]
LOCALID:P-03-247
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