An ab initio exploratory study on the conformational features of the dipeptide MeCO-Ala-Ala-NH-Me in its four different configurations: determination of the behaviour of d-enantiomer amino acids within a peptide chain

Ab initio conformational studies at the RHF/3-21G level of theory were carried out for the dipeptide MeCO-Ala-Ala-NH-Me in its four different configurations (MeCO- l-Ala- l-Ala-NH-Me, MeCO- d-Ala- d-Ala-NH-Me, MeCO- l-Ala- d-Ala-NH-Me and MeCO- d-Ala- l-Ala-NH-Me). From this method the conformations...

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Bibliographic Details
Published in:	Journal of molecular structure. Theochem Vol. 666; pp. 291 - 301
Main Authors:	Brijbassi, Sonya U, Sahai, Michelle A, Setiadi, David H, Chass, Gregory A, Penke, Botond, Csizmadia, Imre G
Format:	Journal Article
Language:	English
Published:	Elsevier B.V 29-12-2003
Subjects:	Ab initio d-Enantiomer Dipeptides l-Enantiomer Protein folding Ramachandran maps Dipeptides l-Enantiomer Ab initio Protein folding Ramachandran maps d-Enantiomer
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Summary:	Ab initio conformational studies at the RHF/3-21G level of theory were carried out for the dipeptide MeCO-Ala-Ala-NH-Me in its four different configurations (MeCO- l-Ala- l-Ala-NH-Me, MeCO- d-Ala- d-Ala-NH-Me, MeCO- l-Ala- d-Ala-NH-Me and MeCO- d-Ala- l-Ala-NH-Me). From this method the conformations for these dipeptides were found to be β lγ l, β lγ d, β lγ d and β lγ l, respectively. Patterns were investigated on Ramachandran maps to identify annihilated critical points among the four dipeptides to determine whether the d-enantiomer was in fact the ‘mirror image’ of the l-enantiomer dipeptide in addition to determining the role of the d-isomer in the peptide chain. The differences in energies for each conformation were also compared between the dipeptides.
ISSN:	0166-1280 1872-7999
DOI:	10.1016/j.theochem.2003.08.034