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Description of peptide and protein secondary structures employing semiempirical methods
Author(s) -
Möhle Kerstin,
Hofmann HansJörg,
Thiel Walter
Publication year - 2001
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 - 10.1002/1096-987x(20010415)22:5<509::aid-jcc1022>3.0.co;2-k
Subject(s) - ab initio , conformational isomerism , peptide , computational chemistry , chemistry , ab initio quantum chemistry methods , molecule , biochemistry , organic chemistry
Novel semiempirical methods (OM1, OM2) have been employed to study typical elements of secondary structure in peptides and proteins. The calculated geometries and relative stabilities are discussed in comparison to corresponding data from the ab initio MO theory and from the established semiempirical methods AM1 and PM3, respectively. It is shown that the description of the peptide conformers is considerably improved by OM1 and OM2 compared with AM1 and PM3, although in some cases there are still discrepancies with the ab initio data. © 2001 John Wiley & Sons, Inc. J Comput Chem 22: 509–520, 2001