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Journal Article

Description of peptide and protein secondary structures employing semiempirical methods

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons59045

Thiel,  Walter
Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Möhle, K., Hofmann, H.-J., & Thiel, W. (2001). Description of peptide and protein secondary structures employing semiempirical methods. Journal of Computational Chemistry, 22(5), 509-520. doi:10.1002/1096-987X(20010415)22:5<509:AID-JCC1022>3.0.CO;2-K.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-1DBE-D
Abstract
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.