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...

Autores
Zamora, Miguel Angel; Baldoni, Hector Armando; Rodriguez, Ana Maria; Enriz, Ricardo Daniel; Sosa, Carlos P.; Perczel, András; Kucsman, Árpád; Farkas, Ödön; Deretey, Eugen; Vank, Judith C.; Csizmadia, Imre Gyula
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
Fil: Rodriguez, Ana Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
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
Fil: Sosa, Carlos P.. Cray Inc.; Estados Unidos
Fil: Perczel, András. Eötvös University; Hungría
Fil: Kucsman, Árpád. Eötvös University; Hungría
Fil: Farkas, Ödön. Eötvös University; Hungría
Fil: Deretey, Eugen. University of Toronto; Canadá
Fil: Vank, Judith C.. University of Toronto; Canadá
Fil: Csizmadia, Imre Gyula. University of Toronto; Canadá
Materia
L-CYSTEINE DIAMIDES
SIDE-CHAIN POTENTIAL-ENERGY SURFACE
AB INITIO AND DFT GEOMETRY OPTIMIZATION
AIM ANALYSIS
INTRAMOLECULAR HYDROGEN BONDING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/127108
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/127108
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 conformationsZamora, Miguel AngelBaldoni, Hector ArmandoRodriguez, Ana MariaEnriz, Ricardo DanielSosa, Carlos P.Perczel, AndrásKucsman, ÁrpádFarkas, ÖdönDeretey, EugenVank, Judith C.Csizmadia, Imre GyulaL-CYSTEINE DIAMIDESSIDE-CHAIN POTENTIAL-ENERGY SURFACEAB INITIO AND DFT GEOMETRY OPTIMIZATIONAIM ANALYSISINTRAMOLECULAR HYDROGEN BONDINGhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A 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.Fil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; ArgentinaFil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; ArgentinaFil: Rodriguez, Ana Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; ArgentinaFil: 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; ArgentinaFil: Sosa, Carlos P.. Cray Inc.; Estados UnidosFil: Perczel, András. Eötvös University; HungríaFil: Kucsman, Árpád. Eötvös University; HungríaFil: Farkas, Ödön. Eötvös University; HungríaFil: Deretey, Eugen. University of Toronto; CanadáFil: Vank, Judith C.. University of Toronto; CanadáFil: Csizmadia, Imre Gyula. University of Toronto; CanadáNational Research Council Canada-NRC Research Press2002-07-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/127108Zamora, 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; 832-8440008-40421480-3291CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://cdnsciencepub.com/doi/10.1139/v02-076info:eu-repo/semantics/altIdentifier/doi/10.1139/V02-076info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:13:54Zoai:ri.conicet.gov.ar:11336/127108instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:13:54.705CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv 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
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
spellingShingle 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
Zamora, Miguel Angel
L-CYSTEINE DIAMIDES
SIDE-CHAIN POTENTIAL-ENERGY SURFACE
AB INITIO AND DFT GEOMETRY OPTIMIZATION
AIM ANALYSIS
INTRAMOLECULAR HYDROGEN BONDING
title_short 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_sort 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.creator.none.fl_str_mv Zamora, Miguel Angel
Baldoni, Hector Armando
Rodriguez, Ana Maria
Enriz, Ricardo Daniel
Sosa, Carlos P.
Perczel, András
Kucsman, Árpád
Farkas, Ödön
Deretey, Eugen
Vank, Judith C.
Csizmadia, Imre Gyula
author Zamora, Miguel Angel
author_facet Zamora, Miguel Angel
Baldoni, Hector Armando
Rodriguez, Ana Maria
Enriz, Ricardo Daniel
Sosa, Carlos P.
Perczel, András
Kucsman, Árpád
Farkas, Ödön
Deretey, Eugen
Vank, Judith C.
Csizmadia, Imre Gyula
author_role author
author2 Baldoni, Hector Armando
Rodriguez, Ana Maria
Enriz, Ricardo Daniel
Sosa, Carlos P.
Perczel, András
Kucsman, Árpád
Farkas, Ödön
Deretey, Eugen
Vank, Judith C.
Csizmadia, Imre Gyula
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv L-CYSTEINE DIAMIDES
SIDE-CHAIN POTENTIAL-ENERGY SURFACE
AB INITIO AND DFT GEOMETRY OPTIMIZATION
AIM ANALYSIS
INTRAMOLECULAR HYDROGEN BONDING
topic L-CYSTEINE DIAMIDES
SIDE-CHAIN POTENTIAL-ENERGY SURFACE
AB INITIO AND DFT GEOMETRY OPTIMIZATION
AIM ANALYSIS
INTRAMOLECULAR HYDROGEN BONDING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Zamora, Miguel Angel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
Fil: Baldoni, Hector Armando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
Fil: Rodriguez, Ana Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia; Argentina
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
Fil: Sosa, Carlos P.. Cray Inc.; Estados Unidos
Fil: Perczel, András. Eötvös University; Hungría
Fil: Kucsman, Árpád. Eötvös University; Hungría
Fil: Farkas, Ödön. Eötvös University; Hungría
Fil: Deretey, Eugen. University of Toronto; Canadá
Fil: Vank, Judith C.. University of Toronto; Canadá
Fil: Csizmadia, Imre Gyula. University of Toronto; Canadá
description 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.
publishDate 2002
dc.date.none.fl_str_mv 2002-07-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/127108
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
0008-4042
1480-3291
CONICET Digital
CONICET
url http://hdl.handle.net/11336/127108
identifier_str_mv 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
0008-4042
1480-3291
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://cdnsciencepub.com/doi/10.1139/v02-076
info:eu-repo/semantics/altIdentifier/doi/10.1139/V02-076
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv National Research Council Canada-NRC Research Press
publisher.none.fl_str_mv National Research Council Canada-NRC Research Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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