Back
Full-text
Journal article

Effect of single-site mutations on hydrophobic-polar lattice proteins.

  • Shi G Center for Simulational Physics, The University of Georgia, Athens, Georgia 30602, USA.
  • Vogel T Theoretical Division (T-1), Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA.
  • Wüst T Scientific IT Services, ETH Zürich IT Services, 8092 Zürich, Switzerland.
  • Li YW National Center for Computational Sciences, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA.
  • Landau DP Center for Simulational Physics, The University of Georgia, Athens, Georgia 30602, USA.
  • 2014-10-15
Published in:
  • Physical review. E, Statistical, nonlinear, and soft matter physics. - 2014
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Mutation
Protein Conformation
Protein Folding
Proteins
Temperature
English 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.
Language
  • English
Open access status
hybrid
Identifiers
Persistent URL
https://sonar.ch/global/documents/52237
Statistics
Document views: 20 File downloads:
  • Full-text: 0