Peptide models XXVII. An exploratory ab initio study on the 21(st) amino acid side-chain conformations of N-formyl-L-selenocysteinamide (For-L-Sec-NH2) and N-acetyl-L-selenocysteine-N-methylamide (Ac-L-Sec-NHMe) in their gamma(L) backbone conformation
Jc. Vank et al., Peptide models XXVII. An exploratory ab initio study on the 21(st) amino acid side-chain conformations of N-formyl-L-selenocysteinamide (For-L-Sec-NH2) and N-acetyl-L-selenocysteine-N-methylamide (Ac-L-Sec-NHMe) in their gamma(L) backbone conformation, CAN J CHEM, 78(3), 2000, pp. 395-408
Citations number
42
Categorie Soggetti
Chemistry
Journal title
CANADIAN JOURNAL OF CHEMISTRY-REVUE CANADIENNE DE CHIMIE
Selenocysteine is expected to have 9 x 9 = 81 conformations [3 x 3 = 9 back
bone: psi (g(+),a,g(-)) x phi (g(+),a,g(-)) and 3 x 3 = 9 side-chain: chi(1
) (g(+),a,g(-)) x chi(2) (g(+),a,g(-))]. In the present study, all the tors
ional modes of the side-chain (chi(1): rotation about the C-alpha-C-beta an
d chi(2): rotation about the C-beta-Se bonds) were investigated in the rela
xed gamma(L) backbone [(phi,psi); (g(-),g(+))] conformation. Seven out of t
he nine expected minima were found at the RHF/3-21G level of theory for N-f
ormyl-L-selenocysteinamide (For-L-Sec-NH2) and N-acetyl-L-selenocysteine-N-
methylamide (Ac-L-Sec-NHMe). The stabilization energy exerted by the -CH2-S
eH side-chain has been compared with that of -CH2-SH and -CH2-OH. Relative
energies of the various conformers were also obtained via single point calc
ulations at the B3LYP/6-31G(d,p) level of theory. Topological analysis of t
he electron density has been performed by Bader's Atoms in Molecule (AIM) a
pproach using the results. The structures were also optimized at the B3LYP/
6-31+G(d,p) level of theory.