How Single-site Mutation Affects HP Lattice Proteins

ORAL

Abstract

We developed a heuristic method based on Wang-Landau\footnote{T. W\"{u}st and D. P. Landau, J. Chem. Phys. \textbf{137}, 064903 (2012).} and multicanonical sampling for determining the ground-state degeneracy of HP lattice proteins \footnote{K. A. Dill, Biochemistry 24, 1501 (1985); K. F. Lau and K. A. Dill, Macromolecules 22, 3986 (1989). }. Our algorithm allowed the most precise estimations of the (sometimes substantial) ground-state degeneracies of some widely studied HP sequences. We investigated the effects of single-site mutation on specific long HP lattice proteins comprehensively, including structural changes in ground-states, changes of ground-state degeneracy and thermodynamic properties of the systems. Both extremely sensitive and insensitive cases have been observed; consequently, properties such as specific heat, tortuosities etc. may be either largely unaffected or may change significantly due to mutation. More interestingly, mutation can even induce a lower ground-state energy in a few cases.

*Supported by NSF

–

Authors

  • Guangjie Shi

    • The University of Georgia
    • Center for Simulational Physics, The University of Georgia

  • David P Landau

    • Center for Simulational Physics, The University of Georgia

  • Thomas Vogel

    • Theoretical Division, Los Alamos National Laboratory

  • Thomas W\"{u}st

    • Swiss Federal Research Institute WSL

  • Ying Wai Li

    • Oak Ridge National Laboratory