Protein folding of the H0P model: A parallel Wang-Landau study
Conference
·
OSTI ID:1223644
- University of Georgia, Athens, GA
- ETH Zurich, Switzerland
- ORNL
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.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- DE-AC05-00OR22725
- OSTI ID:
- 1223644
- Resource Relation:
- Conference: XXVI IUPAP Conference on Computational Physics, CCP2014, Boston, MA, USA, 20140811, 20140814
- Country of Publication:
- United States
- Language:
- English
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