title: Effect of single-site mutations on hydrophobic-polar lattice proteins.
abstract: 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.
authors.affiliation: Center for Simulational Physics, The University of Georgia, Athens, Georgia 30602, USA.
authors.forename: Guangjie
authors.initials: G
authors.lastname: Shi
authors.affiliation: Theoretical Division (T-1), Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA.
authors.forename: Thomas
authors.initials: T
authors.lastname: Vogel
authors.affiliation: Scientific IT Services, ETH Zürich IT Services, 8092 Zürich, Switzerland.
authors.forename: Thomas
authors.initials: T
authors.lastname: Wüst
authors.affiliation: National Center for Computational Sciences, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA.
authors.forename: Ying Wai
authors.initials: YW
authors.lastname: Li
authors.affiliation: Center for Simulational Physics, The University of Georgia, Athens, Georgia 30602, USA.
authors.forename: David P
authors.initials: DP
authors.lastname: Landau
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D013696:Temperature
chemical_list: D011506:Proteins