dc.creator | Zamora, Miguel Angel | |
dc.creator | Baldoni, Hector Armando | |
dc.creator | Rodriguez, Ana Maria | |
dc.creator | Enriz, Ricardo Daniel | |
dc.creator | Sosa, Carlos P. | |
dc.creator | Perczel, András | |
dc.creator | Kucsman, Árpád | |
dc.creator | Farkas, Ödön | |
dc.creator | Deretey, Eugen | |
dc.creator | Vank, Judith C. | |
dc.creator | Csizmadia, Imre Gyula | |
dc.date.accessioned | 2021-03-02T13:32:47Z | |
dc.date.accessioned | 2022-10-15T08:36:44Z | |
dc.date.available | 2021-03-02T13:32:47Z | |
dc.date.available | 2022-10-15T08:36:44Z | |
dc.date.created | 2021-03-02T13:32:47Z | |
dc.date.issued | 2002-07-01 | |
dc.identifier | Zamora, Miguel Angel; Baldoni, Hector Armando; Rodriguez, Ana Maria; Enriz, Ricardo Daniel; Sosa, Carlos P.; et al.; Peptide model XXVIII: An exploratory ab initio and density functional study on the side-chain-backbone interaction in N-acetyl-L-cysteine-N-methylamide and N-formyl-L-cysteinamide in their γL-backbone conformations; National Research Council Canada-NRC Research Press; Canadian Journal of Chemistry; 80; 7; 1-7-2002; 832-844 | |
dc.identifier | 0008-4042 | |
dc.identifier | http://hdl.handle.net/11336/127108 | |
dc.identifier | 1480-3291 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4365764 | |
dc.description.abstract | A conformational and electronic study on the energetically preferred conformations (γL) of N- and C-protected L-cysteine (P-CONH-CH(CH2SH)-CONH-Q, where P and Q may be H or Me) was carried out. After restraining the backbone (BB) conformation to its global minimum (γL or C7eq), all nine possible side-chain (SC) conformations were subjected to geometry optimization at the HF/3-21G and the B3LYP/6-31G(d,p) levels of theory. Seven of the nine side-chain conformers were located on the potential-energy surface. All conformers were subjected to an AIM (atoms in molecules) analysis. This study indicates that three of the seven optimized conformers exhibited either or both SC → BB- or BB → SC-type intramolecular hydrogen bonding. Five conformers, however, had distances between a proton and a heteroatom that suggested hydrogen bonding. | |
dc.language | eng | |
dc.publisher | National Research Council Canada-NRC Research Press | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://cdnsciencepub.com/doi/10.1139/v02-076 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1139/V02-076 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | L-CYSTEINE DIAMIDES | |
dc.subject | SIDE-CHAIN POTENTIAL-ENERGY SURFACE | |
dc.subject | AB INITIO AND DFT GEOMETRY OPTIMIZATION | |
dc.subject | AIM ANALYSIS | |
dc.subject | INTRAMOLECULAR HYDROGEN BONDING | |
dc.title | Peptide model XXVIII: An exploratory ab initio and density functional study on the side-chain-backbone interaction in N-acetyl-L-cysteine-N-methylamide and N-formyl-L-cysteinamide in their γL-backbone conformations | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |