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• W2046496284 abstract "Ab-initio molecular orbital (MO) calculations on the model peptide, N-methylacetamide (NMA), protonated N-methylacetamide (p-NMA), and two natural dipeptides, glyclyglycine (Gly-Gly) and alanylalanine (Ala-Ala), are reported. Calculations at the STO-3G. 3-21G. and 4–31 G levels account for the predominance of the trans conformation in globular proteins. By use of p-NMA as a model precursor, the formation of the peptide bond is studied by the methods of molecular quantum mechanics. These calculations lead to the conclusion that the trans conformation should predominate, in agreement with the crystal structural data on globular proteins. In order to reduce the amount of computer time required for what are evidently the first ab-initio MO calculations on natural dipeptides, force-field calculations have been employed to obtain the conformational potential energy maps." @default.
• W2046496284 created "2016-06-24" @default.
• W2046496284 creator A5006751388 @default.
• W2046496284 creator A5061295554 @default.
• W2046496284 date "1981-03-05" @default.
• W2046496284 modified "2023-10-16" @default.
• W2046496284 title "Ab-initio molecular orbital study of the cis/trans conformations of the peptide bond" @default.
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• W2046496284 doi "https://doi.org/10.1002/qua.560200710" @default.
• W2046496284 hasPublicationYear "1981" @default.
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