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Conformational analysis of polypeptide chains with the aid of density of states calculations
Author(s) -
Jacchieri Saul G.
Publication year - 1997
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/(sici)1097-461x(1997)65:6<1115::aid-qua10>3.0.co;2-4
Subject(s) - potential energy , range (aeronautics) , chemistry , maxima and minima , pairwise comparison , density of states , maxima , kinetic energy , function (biology) , lennard jones potential , transition state , energy (signal processing) , statistical physics , molecular dynamics , computational chemistry , physics , atomic physics , materials science , condensed matter physics , classical mechanics , quantum mechanics , mathematics , art , mathematical analysis , composite material , biology , biochemistry , evolutionary biology , art history , catalysis , statistics , performance art
A model system whose density of states is an analytical function of the potential energy is obtained by combining potential energy wells given by Lennard‐Jones 6‐12 potentials representing pairwise interactions between atoms and circular barriers. Structural aspects of polypeptide chains such as sharp and broad energy extremes and close‐packed and loose‐packed conformations are simulated. By changing Lennard‐Jones parameters, the density of states is described as a function of topological features of the potential energy surface and rules used to interpret density of states calculations are derived. Important results are that the number of clusters of density of states maxima in a given energy range approaches the number of conformational families and very low density of states gaps indicate the existence of kinetic barriers. These conclusions are applied to the conformational analysis of α‐MSH. Structural implications are discussed. © 1997 John Wiley & Sons, Inc. Int J Quant Chem 65 : 1115–1124, 1997