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Title: Protein folding of the H0P model: A parallel Wang-Landau study

We propose a simple modication to the hydrophobic-polar (HP) protein model, by introducing a new type of monomer, "0", with intermediate hydrophobicity of some amino acids between H and P. With the replica-exchange Wang-Landau sampling method, we investigate some widely studied HP sequences as well as their H0P counterparts and observe that the H0P sequences exhibit dramatically reduced ground state degeneracy and more signicant transition signals at low temperature for some thermodynamic properties, such as the specific heat.
Authors:
 [1] ;  [2] ;  [3] ;  [1]
  1. University of Georgia, Athens, GA
  2. ETH Zurich, Switzerland
  3. ORNL
Publication Date:
OSTI Identifier:
1223644
DOE Contract Number:
DE-AC05-00OR22725
Resource Type:
Conference
Resource Relation:
Conference: XXVI IUPAP Conference on Computational Physics, CCP2014, Boston, MA, USA, 20140811, 20140814
Research Org:
Oak Ridge National Laboratory (ORNL)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English