Exact sequence analysis for three-dimensional hydrophobic-polar lattice proteins
نویسندگان
چکیده
منابع مشابه
Exact sequence analysis for three-dimensional hydrophobic-polar lattice proteins.
We have exactly enumerated all sequences and conformations of hydrophobic-polar (HP) proteins with chains of up to 19 monomers on the simple cubic lattice. For two variants of the HP model, where only two types of monomers are distinguished, we determined and statistically analyzed designing sequences, i.e., sequences that have a nondegenerate ground state. Furthermore we were interested in cha...
متن کاملExact Sequence Analysis for Three-Dimensional HP Lattice Proteins
We have exactly enumerated all sequences and conformations of HP proteins with chains of up to 19 monomers on the simple cubic lattice. For two variants of the hydrophobic-polar (HP) model, where only two types of monomers are distinguished, we determined and statistically analyzed designing sequences, i.e., sequences that have a non-degenerate ground state. Furthermore we were interested in ch...
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We present an algorithm for the exhaustive enumeration of all monomer sequences and conformations of short lattice proteins as described by the hydrophobic–polar (HP) model. The algorithm is used for an exact identification of all designing sequences of HP proteins consisting of up to 19 monomers whose conformations are represented by interacting self–avoiding walks on the simple cubic lattice....
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The thermodynamic behavior and structural properties of hydrophobic-polar (HP) lattice proteins interacting with attractive surfaces are studied by means of Wang-Landau sampling. Three benchmark HP sequences (48mer, 67mer, and 103mer) are considered with different types of surfaces, each of which attract either all monomers, only hydrophobic (H) monomers, or only polar (P) monomers, respectivel...
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ژورنال
عنوان ژورنال: The Journal of Chemical Physics
سال: 2005
ISSN: 0021-9606,1089-7690
DOI: 10.1063/1.1814941