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Pair interaction energy decomposition analysis
Author(s) -
Fedorov Dmitri G.,
Kitaura Kazuo
Publication year - 2006
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20496
Subject(s) - chemistry , interaction energy , decomposition , protein data bank (rcsb pdb) , molecule , fragment molecular orbital , computational chemistry , ab initio , molecular orbital , stereochemistry , organic chemistry
The energy decomposition analysis (EDA) by Kitaura and Morokuma was redeveloped in the framework of the fragment molecular orbital method (FMO). The proposed pair interaction energy decomposition analysis (PIEDA) can treat large molecular clusters and the systems in which fragments are connected by covalent bonds, such as proteins. The interaction energy in PIEDA is divided into the same contributions as in EDA: the electrostatic, exchange‐repulsion, and charge transfer energies, to which the correlation (dispersion) term was added. The careful comparison to the ab initio EDA interaction energies for water clusters with 2–16 molecules revealed that PIEDA has the error of at most 1.2 kcal/mol (or about 1%). The analysis was applied to (H 2 O) 1024 , the α helix, β turn, and β strand of polyalanine (ALA) 10 , as well as to the synthetic protein (PDB code 1L2Y) with 20 residues. The comparative aspects of the polypeptide isomer stability are discussed in detail. © 2006 Wiley Periodicals, Inc.J Comput Chem 2007