Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH

Autores
Vila, Jorge Alberto; Arnautova, Yelena A.; Vorobjev, Yury; Scheraga, Harold A.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A method is proposed to determine the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH, provided that the observed and chemical shifts and the protein structure, or the fraction of H(+) form, are known. This method is based on the use of quantum chemical methods to compute the (13)C NMR shieldings of all the imidazole ring carbons ((13)C(γ), , and ) for each of the two tautomers, N(δ1)-H and N(ε2)-H, and the protonated form, H(+), of histidine. This methodology enabled us (i) to determine the fraction of all the tautomeric forms of histidine for eight proteins for which the and chemical shifts had been determined in solution in the pH range of 3.2 to 7.5 and (ii) to estimate the fraction of tautomeric forms of eight histidine-containing dipeptide crystals for which the chemical shifts had been determined by solid-state (13)C NMR. Our results for proteins indicate that the protonated form is the most populated one, whereas the distribution of the tautomeric forms for the imidazole ring varies significantly among different histidines in the same protein, reflecting the importance of the environment of the histidines in determining the tautomeric forms. In addition, for ∼70% of the neutral histidine-containing dipeptides, the method leads to fairly good agreement between the calculated and the experimental tautomeric form. Coexistence of different tautomeric forms in the same crystal structure may explain the remaining 30% of disagreement.
Fil: Vila, Jorge Alberto. Cornell University; Estados Unidos. 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 ; Argentina
Fil: Arnautova, Yelena A.. Cornell University; Estados Unidos
Fil: Vorobjev, Yury. Russian Academy of Science; Rusia
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
Materia
Histidine Protonation
Histidine Tautomers
Ph Effect
Side Chain Conformation
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:11336/15587
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pHVila, Jorge AlbertoArnautova, Yelena A.Vorobjev, YuryScheraga, Harold A.Histidine ProtonationHistidine TautomersPh EffectSide Chain Conformationhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1A method is proposed to determine the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH, provided that the observed and chemical shifts and the protein structure, or the fraction of H(+) form, are known. This method is based on the use of quantum chemical methods to compute the (13)C NMR shieldings of all the imidazole ring carbons ((13)C(γ), , and ) for each of the two tautomers, N(δ1)-H and N(ε2)-H, and the protonated form, H(+), of histidine. This methodology enabled us (i) to determine the fraction of all the tautomeric forms of histidine for eight proteins for which the and chemical shifts had been determined in solution in the pH range of 3.2 to 7.5 and (ii) to estimate the fraction of tautomeric forms of eight histidine-containing dipeptide crystals for which the chemical shifts had been determined by solid-state (13)C NMR. Our results for proteins indicate that the protonated form is the most populated one, whereas the distribution of the tautomeric forms for the imidazole ring varies significantly among different histidines in the same protein, reflecting the importance of the environment of the histidines in determining the tautomeric forms. In addition, for ∼70% of the neutral histidine-containing dipeptides, the method leads to fairly good agreement between the calculated and the experimental tautomeric form. Coexistence of different tautomeric forms in the same crystal structure may explain the remaining 30% of disagreement.Fil: Vila, Jorge Alberto. Cornell University; Estados Unidos. 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 ; ArgentinaFil: Arnautova, Yelena A.. Cornell University; Estados UnidosFil: Vorobjev, Yury. Russian Academy of Science; RusiaFil: Scheraga, Harold A.. Cornell University; Estados UnidosNational Academy of Sciences2011-04-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/15587Vila, Jorge Alberto; Arnautova, Yelena A.; Vorobjev, Yury; Scheraga, Harold A.; Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 14; 5-4-2011; 5602-56070027-84241091-6490enginfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1102373108info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078339/info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/108/14/5602info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:11:43Zoai:ri.conicet.gov.ar:11336/15587instacron: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:34982025-09-29 10:11:43.525CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
title Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
spellingShingle Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
Vila, Jorge Alberto
Histidine Protonation
Histidine Tautomers
Ph Effect
Side Chain Conformation
title_short Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
title_full Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
title_fullStr Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
title_full_unstemmed Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
title_sort Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH
dc.creator.none.fl_str_mv Vila, Jorge Alberto
Arnautova, Yelena A.
Vorobjev, Yury
Scheraga, Harold A.
author Vila, Jorge Alberto
author_facet Vila, Jorge Alberto
Arnautova, Yelena A.
Vorobjev, Yury
Scheraga, Harold A.
author_role author
author2 Arnautova, Yelena A.
Vorobjev, Yury
Scheraga, Harold A.
author2_role author
author
author
dc.subject.none.fl_str_mv Histidine Protonation
Histidine Tautomers
Ph Effect
Side Chain Conformation
topic Histidine Protonation
Histidine Tautomers
Ph Effect
Side Chain Conformation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A method is proposed to determine the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH, provided that the observed and chemical shifts and the protein structure, or the fraction of H(+) form, are known. This method is based on the use of quantum chemical methods to compute the (13)C NMR shieldings of all the imidazole ring carbons ((13)C(γ), , and ) for each of the two tautomers, N(δ1)-H and N(ε2)-H, and the protonated form, H(+), of histidine. This methodology enabled us (i) to determine the fraction of all the tautomeric forms of histidine for eight proteins for which the and chemical shifts had been determined in solution in the pH range of 3.2 to 7.5 and (ii) to estimate the fraction of tautomeric forms of eight histidine-containing dipeptide crystals for which the chemical shifts had been determined by solid-state (13)C NMR. Our results for proteins indicate that the protonated form is the most populated one, whereas the distribution of the tautomeric forms for the imidazole ring varies significantly among different histidines in the same protein, reflecting the importance of the environment of the histidines in determining the tautomeric forms. In addition, for ∼70% of the neutral histidine-containing dipeptides, the method leads to fairly good agreement between the calculated and the experimental tautomeric form. Coexistence of different tautomeric forms in the same crystal structure may explain the remaining 30% of disagreement.
Fil: Vila, Jorge Alberto. Cornell University; Estados Unidos. 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 ; Argentina
Fil: Arnautova, Yelena A.. Cornell University; Estados Unidos
Fil: Vorobjev, Yury. Russian Academy of Science; Rusia
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
description A method is proposed to determine the fraction of the tautomeric forms of the imidazole ring of histidine in proteins as a function of pH, provided that the observed and chemical shifts and the protein structure, or the fraction of H(+) form, are known. This method is based on the use of quantum chemical methods to compute the (13)C NMR shieldings of all the imidazole ring carbons ((13)C(γ), , and ) for each of the two tautomers, N(δ1)-H and N(ε2)-H, and the protonated form, H(+), of histidine. This methodology enabled us (i) to determine the fraction of all the tautomeric forms of histidine for eight proteins for which the and chemical shifts had been determined in solution in the pH range of 3.2 to 7.5 and (ii) to estimate the fraction of tautomeric forms of eight histidine-containing dipeptide crystals for which the chemical shifts had been determined by solid-state (13)C NMR. Our results for proteins indicate that the protonated form is the most populated one, whereas the distribution of the tautomeric forms for the imidazole ring varies significantly among different histidines in the same protein, reflecting the importance of the environment of the histidines in determining the tautomeric forms. In addition, for ∼70% of the neutral histidine-containing dipeptides, the method leads to fairly good agreement between the calculated and the experimental tautomeric form. Coexistence of different tautomeric forms in the same crystal structure may explain the remaining 30% of disagreement.
publishDate 2011
dc.date.none.fl_str_mv 2011-04-05
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/11336/15587
Vila, Jorge Alberto; Arnautova, Yelena A.; Vorobjev, Yury; Scheraga, Harold A.; Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 14; 5-4-2011; 5602-5607
0027-8424
1091-6490
url http://hdl.handle.net/11336/15587
identifier_str_mv Vila, Jorge Alberto; Arnautova, Yelena A.; Vorobjev, Yury; Scheraga, Harold A.; Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 108; 14; 5-4-2011; 5602-5607
0027-8424
1091-6490
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.1102373108
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078339/
info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/108/14/5602
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 Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
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 13.070432

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