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

Autor:	Marcelo F. Masman, Ricardo D. Enriz, Nelida Maria Peruchena, N. G. Fidanza, Ana M. Rodríguez, Imre G. Csizmadia, M.A. Zamora
Rok vydání:	2002
Předmět:	Bond length chemistry.chemical_classification Crystallography Molecular geometry Chemistry Ab initio quantum chemistry methods Ab initio Molecule Density functional theory Methylamide Atomic and Molecular Physics and Optics Amino acid
Zdroj:	The European Physical Journal D. 20:531-542
ISSN:	1434-6079 1434-6060
DOI:	10.1140/epjd/e2002-00150-y
Popis:	A conformational and electronic study on N-acetyl-L-glutamate-N-methylamide was carried out. Theoretical computational analysis revealed 21 different 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 different conformational behaviour in comparison with other amino acids possessing shorter side-chains. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::95d84574fbfac73a63ca4b403f01ffd7 https://doi.org/10.1140/epjd/e2002-00150-y Zobrazit plný text záznamu Full text from SpringerLink