Further evidence for the absence of persistent polyproline II conformation in the XAO peptide

Autores
Makowska, Joanna; Rodziewicz-Motowidlo, Sylwia; Baginska, Katarzyna; Makowski, Mariusz; Vila, Jorge Alberto; Liwo, Adam; Chmurzynski, Lech; Scheraga, Harold A.
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It has been suggested that the alanine-based peptide with sequence Ac-XX-[A]7-OO-NH2, termed XAO where X denotes diaminobutyric acid and O denotes ornithine, exists in a predominantly polyproline-helix (PII) conformation in aqueous solution. In our recent work, we demonstrated that this “polyproline conformation” should be regarded as a set of local conformational states rather than as the overall conformation of the molecule. In this work, we present further evidence to support this statement. Differential scanning calorimetry measurements showed only a very small peak in the heat capacity of an aqueous solution of XAO at 57°C, whereas the suggested transition to the PII structure should occur at ∼30°C. We also demonstrate that the temperature dependence of the 3JHNHα coupling constants of the alanine residues can be explained qualitatively in terms of Boltzmann averaging over all local conformational states; therefore, this temperature dependence proves that a conformational transition does not occur. Canonical MD simulations with the solvent represented by the generalized Born model, and with time-averaged NMR-derived restraints, demonstrate the presence of an ensemble of structures with a substantial amount of local PII conformational states but not with an overall PII conformation.
Fil: Makowska, Joanna. Uniwersytet Gdanski; Polonia. Cornell University; Estados Unidos
Fil: Rodziewicz-Motowidlo, Sylwia. Uniwersytet Gdanski; Polonia. Cornell University; Estados Unidos
Fil: Baginska, Katarzyna. Uniwersytet Gdanski; Polonia
Fil: Makowski, Mariusz. Cornell University; Estados Unidos. Uniwersytet Gdanski; Polonia
Fil: Vila, Jorge Alberto. 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. Cornell University; Estados Unidos
Fil: Liwo, Adam. Cornell University; Estados Unidos
Fil: Chmurzynski, Lech. Uniwersytet Gdanski; Polonia
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
Materia
Polyproline II
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:11336/135153
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/135153
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Further evidence for the absence of persistent polyproline II conformation in the XAO peptideMakowska, JoannaRodziewicz-Motowidlo, SylwiaBaginska, KatarzynaMakowski, MariuszVila, Jorge AlbertoLiwo, AdamChmurzynski, LechScheraga, Harold A.Polyproline IIhttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1It has been suggested that the alanine-based peptide with sequence Ac-XX-[A]7-OO-NH2, termed XAO where X denotes diaminobutyric acid and O denotes ornithine, exists in a predominantly polyproline-helix (PII) conformation in aqueous solution. In our recent work, we demonstrated that this “polyproline conformation” should be regarded as a set of local conformational states rather than as the overall conformation of the molecule. In this work, we present further evidence to support this statement. Differential scanning calorimetry measurements showed only a very small peak in the heat capacity of an aqueous solution of XAO at 57°C, whereas the suggested transition to the PII structure should occur at ∼30°C. We also demonstrate that the temperature dependence of the 3JHNHα coupling constants of the alanine residues can be explained qualitatively in terms of Boltzmann averaging over all local conformational states; therefore, this temperature dependence proves that a conformational transition does not occur. Canonical MD simulations with the solvent represented by the generalized Born model, and with time-averaged NMR-derived restraints, demonstrate the presence of an ensemble of structures with a substantial amount of local PII conformational states but not with an overall PII conformation.Fil: Makowska, Joanna. Uniwersytet Gdanski; Polonia. Cornell University; Estados UnidosFil: Rodziewicz-Motowidlo, Sylwia. Uniwersytet Gdanski; Polonia. Cornell University; Estados UnidosFil: Baginska, Katarzyna. Uniwersytet Gdanski; PoloniaFil: Makowski, Mariusz. Cornell University; Estados Unidos. Uniwersytet Gdanski; PoloniaFil: Vila, Jorge Alberto. 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. Cornell University; Estados UnidosFil: Liwo, Adam. Cornell University; Estados UnidosFil: Chmurzynski, Lech. Uniwersytet Gdanski; PoloniaFil: Scheraga, Harold A.. Cornell University; Estados UnidosCell Press2007-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/135153Makowska, Joanna; Rodziewicz-Motowidlo, Sylwia; Baginska, Katarzyna; Makowski, Mariusz; Vila, Jorge Alberto; et al.; Further evidence for the absence of persistent polyproline II conformation in the XAO peptide; Cell Press; Biophysical Journal; 92; 8; 4-2007; 2904-29170006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.106.097550info:eu-repo/semantics/altIdentifier/url/https://www.cell.com/biophysj/fulltext/S0006-3495(07)71094-9info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:37:50Zoai:ri.conicet.gov.ar:11336/135153instacron: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:34982025-10-15 15:37:50.638CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
title Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
spellingShingle Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
Makowska, Joanna
Polyproline II
title_short Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
title_full Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
title_fullStr Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
title_full_unstemmed Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
title_sort Further evidence for the absence of persistent polyproline II conformation in the XAO peptide
dc.creator.none.fl_str_mv Makowska, Joanna
Rodziewicz-Motowidlo, Sylwia
Baginska, Katarzyna
Makowski, Mariusz
Vila, Jorge Alberto
Liwo, Adam
Chmurzynski, Lech
Scheraga, Harold A.
author Makowska, Joanna
author_facet Makowska, Joanna
Rodziewicz-Motowidlo, Sylwia
Baginska, Katarzyna
Makowski, Mariusz
Vila, Jorge Alberto
Liwo, Adam
Chmurzynski, Lech
Scheraga, Harold A.
author_role author
author2 Rodziewicz-Motowidlo, Sylwia
Baginska, Katarzyna
Makowski, Mariusz
Vila, Jorge Alberto
Liwo, Adam
Chmurzynski, Lech
Scheraga, Harold A.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Polyproline II
topic Polyproline II
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv It has been suggested that the alanine-based peptide with sequence Ac-XX-[A]7-OO-NH2, termed XAO where X denotes diaminobutyric acid and O denotes ornithine, exists in a predominantly polyproline-helix (PII) conformation in aqueous solution. In our recent work, we demonstrated that this “polyproline conformation” should be regarded as a set of local conformational states rather than as the overall conformation of the molecule. In this work, we present further evidence to support this statement. Differential scanning calorimetry measurements showed only a very small peak in the heat capacity of an aqueous solution of XAO at 57°C, whereas the suggested transition to the PII structure should occur at ∼30°C. We also demonstrate that the temperature dependence of the 3JHNHα coupling constants of the alanine residues can be explained qualitatively in terms of Boltzmann averaging over all local conformational states; therefore, this temperature dependence proves that a conformational transition does not occur. Canonical MD simulations with the solvent represented by the generalized Born model, and with time-averaged NMR-derived restraints, demonstrate the presence of an ensemble of structures with a substantial amount of local PII conformational states but not with an overall PII conformation.
Fil: Makowska, Joanna. Uniwersytet Gdanski; Polonia. Cornell University; Estados Unidos
Fil: Rodziewicz-Motowidlo, Sylwia. Uniwersytet Gdanski; Polonia. Cornell University; Estados Unidos
Fil: Baginska, Katarzyna. Uniwersytet Gdanski; Polonia
Fil: Makowski, Mariusz. Cornell University; Estados Unidos. Uniwersytet Gdanski; Polonia
Fil: Vila, Jorge Alberto. 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. Cornell University; Estados Unidos
Fil: Liwo, Adam. Cornell University; Estados Unidos
Fil: Chmurzynski, Lech. Uniwersytet Gdanski; Polonia
Fil: Scheraga, Harold A.. Cornell University; Estados Unidos
description It has been suggested that the alanine-based peptide with sequence Ac-XX-[A]7-OO-NH2, termed XAO where X denotes diaminobutyric acid and O denotes ornithine, exists in a predominantly polyproline-helix (PII) conformation in aqueous solution. In our recent work, we demonstrated that this “polyproline conformation” should be regarded as a set of local conformational states rather than as the overall conformation of the molecule. In this work, we present further evidence to support this statement. Differential scanning calorimetry measurements showed only a very small peak in the heat capacity of an aqueous solution of XAO at 57°C, whereas the suggested transition to the PII structure should occur at ∼30°C. We also demonstrate that the temperature dependence of the 3JHNHα coupling constants of the alanine residues can be explained qualitatively in terms of Boltzmann averaging over all local conformational states; therefore, this temperature dependence proves that a conformational transition does not occur. Canonical MD simulations with the solvent represented by the generalized Born model, and with time-averaged NMR-derived restraints, demonstrate the presence of an ensemble of structures with a substantial amount of local PII conformational states but not with an overall PII conformation.
publishDate 2007
dc.date.none.fl_str_mv 2007-04
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/11336/135153
Makowska, Joanna; Rodziewicz-Motowidlo, Sylwia; Baginska, Katarzyna; Makowski, Mariusz; Vila, Jorge Alberto; et al.; Further evidence for the absence of persistent polyproline II conformation in the XAO peptide; Cell Press; Biophysical Journal; 92; 8; 4-2007; 2904-2917
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/135153
identifier_str_mv Makowska, Joanna; Rodziewicz-Motowidlo, Sylwia; Baginska, Katarzyna; Makowski, Mariusz; Vila, Jorge Alberto; et al.; Further evidence for the absence of persistent polyproline II conformation in the XAO peptide; Cell Press; Biophysical Journal; 92; 8; 4-2007; 2904-2917
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.106.097550
info:eu-repo/semantics/altIdentifier/url/https://www.cell.com/biophysj/fulltext/S0006-3495(07)71094-9
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 Cell Press
publisher.none.fl_str_mv Cell 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
_version_ 1846083498218094592
score 12.891075

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