Effect of Single-Site Mutations on HP Lattice Proteins

Journal Article · Wed Jan 01 00:00:00 EST 2014 · Physical Review E

DOI:https://doi.org/10.1103/PhysRevE.90.033307· OSTI ID:1157114

Shi, Guangjie ^[1]; Vogel, Thomas ^[2]; Wuest, Thomas ^[3]; Li, Ying Wai ^[4]; Landau, David P ^[1]

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1. University of Georgia, Athens, GA
2. Los Alamos National Laboratory (LANL)
3. Swiss Federal Research Institute, Switzerland
4. ORNL

We developed a heuristic method for determining the ground-state degeneracy of hydrophobic-polar (HP) lattice proteins, based on Wang-Landau and multicanonical sampling. It is applied during comprehensive studies of single-site mutations in specific HP proteins with different sequences. The effects in which we are interested include structural changes in ground-states, changes of ground-state energy, degeneracy, and thermodynamic properties of the system. With respect to mutations, both extremely sensitive and insensitive positions in the HP sequence have been found. That is, ground state energies and degeneracies, as well as other thermodynamic and structural quantities may be either largely unaffected or may change significantly due to mutation.

• Research Organization: Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
• Sponsoring Organization: USDOE Office of Science (SC)
• DOE Contract Number: DE-AC05-00OR22725
• OSTI ID: 1157114
• Journal Information: Physical Review E, Vol. 90, Issue 3; ISSN 1539--3755
• Country of Publication: United States
• Language: English