Exploration of the full conformational space of N-acetyl-L-glutamate-N-methylamide

M.F MASMAN.; M.A.ZAMORA; A.M RODRIGUEZ; N.G.FIDANZA; N.PERUCHENA; ENRIZ R.D.; I.G. CSIZMADIA

EUROPEAN JOURNAL OF PHYSICS

IOP PUBLISHING LTD

Lugar: Londres; Año: 2002 vol. 20 p. 531 - 542

0143-0807

A conformational and electronic study on N-acetyl-L-glutamate-N-methylamide was carried out. Theoretical computational analysis revealed 21 dierent conformations at the RB3LYP/6-31G(d) level of theory. Ab initio calculations at two levels of theory (RHF/3-21G and RHF/6-31G(d)) were also performed. All side-chain conformations were explored for this compound. N-acetyl-L-glutamate-N-methylamide displayed a dierent conformational behaviour in comparison with other amino acids possessing shorter sidechains. These results can be attributed, at least in part, to the side-chain-backbone interactions, which are stabilizing the low-energy conformations in this molecule.