Mostrar el registro sencillo del ítem

dc.contributor.author
Koo, Joseph C.P.  
dc.contributor.author
Lam, Janice S.W.  
dc.contributor.author
Salpietro, Salvatore J.  
dc.contributor.author
Chass, Gregory A.  
dc.contributor.author
Enriz, Ricardo Daniel  
dc.contributor.author
Torday, Ladislaus L.  
dc.contributor.author
Varro, Andras  
dc.contributor.author
Papp, Julius Gy.  
dc.date.available
2021-07-16T01:01:12Z  
dc.date.issued
2002-12  
dc.identifier.citation
Koo, Joseph C.P.; Lam, Janice S.W.; Salpietro, Salvatore J.; Chass, Gregory A.; Enriz, Ricardo Daniel; et al.; How reliable could economic Hartree-Fock computations be in studying large, folded peptides? A comparative HF and DFT case study on N- and C-protected aspartic acid; Elsevier Science; Journal of Molecular Structure Theochem; 619; 1-3; 12-2002; 143-194  
dc.identifier.issn
0166-1280  
dc.identifier.uri
http://hdl.handle.net/11336/136295  
dc.description.abstract
In this study, potential energy hypersurfaces have been generated and analyzed for each of the nine possible backbone (BB) conformations for both the endo and exo forms of N-acetyl-L-aspartic acid N′-methylamide. Ab initio calculations were carried out at RHF/3-21G, RHF/6-31G(d), and B3LYP/6-31G(d) levels for all backbone conformations. The relative energies, as well as stabilization energies exerted by the sidechain (SC) on the backbone, were calculated for all stable conformers. All sidechain-sidechain (HO···O=C), backbone-backbone (N-H⋯O=C), and sidechain-backbone (N-H···O=C; N-H···OH) hydrogen bond interactions were analyzed. The appearance of the traditionally absent αL and εL conformers may be recognized as special geometric orientation which the aspartyl residue manifests during peptide folding or ligand docking in a receptor that contains aspartic acids in its ligand recognition sites. At all three levels of theory, there exists a trend between the hydrogen bond distance and ring size. In addition, strikingly high correlations between the torsional angles (R2 = 0.9937 for RHF/6-31G(d) versus RHF/3-21G; R2 = 0.9967 for B3LYP/6-31G(d) versus RHF/6-31G(d); R2 = 0.9914 for B3LYP/6-31G(d) versus RHF/3-21G) and between the ΔE values in kcal/mol (R2 = 0.9424 for RHF/6-31G(d) versus RHF/3-21G; R2 = 0.9108 for B3LYP/6-31G(d) versus RHF/6-31G(d); R2 = 0.9434 B3LYP/6-31G(d) versus RHF/3-21G) found at the different ab initio levels suggest that calculations carried out at the lower levels (i.e. at RHF/3-21G) are still significant.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
ASPARTIC ACID RESIDUE  
dc.subject
DENSITY FUNCTIONAL THEORY CONFORMATIONS  
dc.subject
EXTERNAL HYDROGEN BONDING  
dc.subject
HELICAL STRUCTURE  
dc.subject
INTERNAL HYDROGEN BONDING  
dc.subject
ΑL  
dc.subject
ΕL HELICAL STRUCTURE  
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica  
dc.subject.classification
Ciencias Químicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
How reliable could economic Hartree-Fock computations be in studying large, folded peptides? A comparative HF and DFT case study on N- and C-protected aspartic acid  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2021-02-17T20:11:37Z  
dc.journal.volume
619  
dc.journal.number
1-3  
dc.journal.pagination
143-194  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Koo, Joseph C.P.. University of Toronto; Canadá  
dc.description.fil
Fil: Lam, Janice S.W.. University of Toronto; Canadá  
dc.description.fil
Fil: Salpietro, Salvatore J.. University of Toronto; Canadá  
dc.description.fil
Fil: Chass, Gregory A.. University of Toronto; Canadá. Velocet R And D; Canadá  
dc.description.fil
Fil: Enriz, Ricardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis. Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Química; Argentina  
dc.description.fil
Fil: Torday, Ladislaus L.. Szegedi Tudományegyetem; Hungría  
dc.description.fil
Fil: Varro, Andras. Szegedi Tudományegyetem; Hungría  
dc.description.fil
Fil: Papp, Julius Gy.. Szegedi Tudományegyetem; Hungría  
dc.journal.title
Journal of Molecular Structure Theochem  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0166128002005791  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/S0166-1280(02)00579-1