{'fraction_non_alphanumeric': 0.052450558899398106, 'fraction_numerical': 0.03353396388650043, 'mean_word_length': 4.938775510204081, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 1, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Adjusting potential energy functions for lattice models of chain molecules

Lattice models of proteins can approximate off‐lattice structures to arbitrary precision with RMS (root mean squared) deviations roughly equal to half the lattice spacing (Rykunov et al., Proteins 22:100–109, 1995; Reva et al., J. Comp. Biol., 1996). However, even small distortions in the positions of chain links lead to significant errors in lattice‐based energy calculations (Reva et al., J. Comp. Chem., 1996). These errors arise mainly from rigid interactions (such as steric repulsion) which change their energies considerably at a range which is much smaller than the usual accuracy of lattice modeling (>1.0 Å). To reduce this error, we suggest a procedure of adjusting energy functions to a given lattice. The general approach is illustrated with energy calculations based on pairwise potentials by Kolinski et al. (J. Chem. Phys. 98:1–14, 1993). At all the lattice spacings, from 0.5–3.8 Å, the lattice‐adjusted potentials improve the accuracy of lattice‐based energy calculations and Increase the correlations between off‐lattice and lattice energies. © 1996 Wiley‐Liss, Inc.