A First Look at Structural Properties of Long HP Lattice Protein Sequences

Despite the apparent simplicity of the HP lattice protein model [1], this class of “simple, exact” models has been extensively studied across disciplines due to either an interest in the principles which govern protein folding [2], the NP-complete computational complexity [3], or both. In this work, we use replica exchange Wang-Landau sampling [4] to study two of the longest HP sequences ever studied (209 and 248 monomers) [5,6]. We extract specific heat curves, report ground state energies, and, for the first time, investigate structural properties of interest for these long sequences. We qualitatively compare the thermodynamics, ground state structures, and structural transitions of these long sequences to each-other and to shorter sequences [7].

 

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[6] A. C. K. Farris and D. P. Landau, Physica A 569, 125778 (2021)

[7] T. Wüst and D. P. Landau, J. Chem. Phys. 137 (6) 064903 (2012)