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Monte carlo simulations of protein folding. I. Lattice model and interaction scheme
Author(s) -
Kolinski Andrzej,
Skolnick Jeffrey
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340180405
Subject(s) - monte carlo method , globular protein , statistical physics , lattice (music) , protein folding , lattice protein , physics , crystallography , biological system , chemistry , mathematics , statistics , biology , nuclear magnetic resonance , acoustics
A new hierarchical method for the simulation of the protein folding process and the de novo prediction of protein three‐dimensional structure is proposed. The reduced representation of the protein α‐carbon backbone employs lattice discretizations of increasing geometrical resolution and a single ball representation of side chain rotamers. In particular, coarser and finer lattice backbone descriptions are used. The coarser (finer) lattice represents Cα traces of native proteins with an accuracy of 1.0 (0.7) Å rms. Folding is simulated by means of very fast Monte Carlo lattice dynamics. The potential of mean force, predominantly of statistical origin, contains several novel terms that facilitate the cooperative assembly of secondary structure elements and the cooperative packing of the side chains. Particular contributions to the interaction scheme are discussed in detail. In the accompanying paper (Kolinski, A., Skolnick, J. Monte Carlo simulation of protein folding. II. Application to protein A, ROP, and crambin. Proteins 18:353–366, 1994), the method is applied to three small globular proteins. © 1994 John Wiley & Sons, Inc.