Conformational transitions of a confined lattice protein: A Wang-Landau study

We use Wang-Landau sampling with suitable Monte Carlo trial moves to study a hydrophobic-polar (HP) lattice protein confined between two parallel, attractive walls. The density of states is determined iteratively by a random walk in energy space. Thermodynamic and structural properties, such as spec...

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Bibliographic Details
Published inJournal of physics. Conference series Vol. 402; no. 1; pp. 12048 - 8
Main Authors Pattanasiri, Busara, Li, Ying Wai, Landau, David P, Wüst, Thomas, Triampo, Wannapong
Format Journal Article
LanguageEnglish
Published Bristol IOP Publishing 20.12.2012
Subjects
Attraction
Collapse
Hydrophobicity
Lattices
Monomers
Monte Carlo methods
Physics
Proteins
Random walk
Sampling
Surface chemistry
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Summary:We use Wang-Landau sampling with suitable Monte Carlo trial moves to study a hydrophobic-polar (HP) lattice protein confined between two parallel, attractive walls. The density of states is determined iteratively by a random walk in energy space. Thermodynamic and structural properties, such as specific heat, number of surface contacts and number of H-H monomer pairs, are then calculated. When the surface attraction is comparable to the internal attraction among the hydrophobic monomers in the chain, two conformational “transitions”, adsorption at higher temperature and collapse at lower temperature, have been analyzed based on these properties. This transition behavior depends on the variation of surface separation.
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ISSN:1742-6588
1742-6596
DOI:10.1088/1742-6596/402/1/012048