External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations

Autores
Schwaighofer, Andreas; Alcaraz, Mirta Raquel; Araman, Can; Goicoechea, Hector Casimiro; Lendl, Bernhard
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of protein secondary structure. The use of CD spectroscopy is limited to low protein concentrations (<2 mg ml−1), while FTIR spectroscopy is commonly used in a higher concentration range (>5 mg ml−1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of protein and polypeptide secondary structure at concentrations as low as 0.25 mg ml−1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The concentration dependence of the α-β transition temperature between 0.25 and 10 mg ml−1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same concentration range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.
Fil: Schwaighofer, Andreas. Technische Universitat Wien; Austria
Fil: Alcaraz, Mirta Raquel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Araman, Can. University Of Vienna; Austria
Fil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina
Fil: Lendl, Bernhard. Technische Universitat Wien; Austria
Materia
BIOANALYTICAL CHEMISTRY
INFRARED SPECTROSCOPY
PROTEIN FOLDING
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:11336/111213
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/111213
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrationsSchwaighofer, AndreasAlcaraz, Mirta RaquelAraman, CanGoicoechea, Hector CasimiroLendl, BernhardBIOANALYTICAL CHEMISTRYINFRARED SPECTROSCOPYPROTEIN FOLDINGhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of protein secondary structure. The use of CD spectroscopy is limited to low protein concentrations (<2 mg ml−1), while FTIR spectroscopy is commonly used in a higher concentration range (>5 mg ml−1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of protein and polypeptide secondary structure at concentrations as low as 0.25 mg ml−1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The concentration dependence of the α-β transition temperature between 0.25 and 10 mg ml−1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same concentration range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.Fil: Schwaighofer, Andreas. Technische Universitat Wien; AustriaFil: Alcaraz, Mirta Raquel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Araman, Can. University Of Vienna; AustriaFil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; ArgentinaFil: Lendl, Bernhard. Technische Universitat Wien; AustriaNature Publishing Group2016-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/111213Schwaighofer, Andreas; Alcaraz, Mirta Raquel; Araman, Can ; Goicoechea, Hector Casimiro; Lendl, Bernhard; External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations; Nature Publishing Group; Scientific Reports; 6; 9-2016; 33556-335662045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/srep33556info:eu-repo/semantics/altIdentifier/doi/10.1038/srep33556info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:10Zoai:ri.conicet.gov.ar:11336/111213instacron: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:34982025-09-03 09:52:10.873CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
title External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
spellingShingle External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
Schwaighofer, Andreas
BIOANALYTICAL CHEMISTRY
INFRARED SPECTROSCOPY
PROTEIN FOLDING
title_short External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
title_full External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
title_fullStr External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
title_full_unstemmed External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
title_sort External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations
dc.creator.none.fl_str_mv Schwaighofer, Andreas
Alcaraz, Mirta Raquel
Araman, Can
Goicoechea, Hector Casimiro
Lendl, Bernhard
author Schwaighofer, Andreas
author_facet Schwaighofer, Andreas
Alcaraz, Mirta Raquel
Araman, Can
Goicoechea, Hector Casimiro
Lendl, Bernhard
author_role author
author2 Alcaraz, Mirta Raquel
Araman, Can
Goicoechea, Hector Casimiro
Lendl, Bernhard
author2_role author
author
author
author
dc.subject.none.fl_str_mv BIOANALYTICAL CHEMISTRY
INFRARED SPECTROSCOPY
PROTEIN FOLDING
topic BIOANALYTICAL CHEMISTRY
INFRARED SPECTROSCOPY
PROTEIN FOLDING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of protein secondary structure. The use of CD spectroscopy is limited to low protein concentrations (<2 mg ml−1), while FTIR spectroscopy is commonly used in a higher concentration range (>5 mg ml−1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of protein and polypeptide secondary structure at concentrations as low as 0.25 mg ml−1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The concentration dependence of the α-β transition temperature between 0.25 and 10 mg ml−1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same concentration range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.
Fil: Schwaighofer, Andreas. Technische Universitat Wien; Austria
Fil: Alcaraz, Mirta Raquel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Araman, Can. University Of Vienna; Austria
Fil: Goicoechea, Hector Casimiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química. Cátedra de Química Analítica; Argentina
Fil: Lendl, Bernhard. Technische Universitat Wien; Austria
description Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of protein secondary structure. The use of CD spectroscopy is limited to low protein concentrations (<2 mg ml−1), while FTIR spectroscopy is commonly used in a higher concentration range (>5 mg ml−1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of protein and polypeptide secondary structure at concentrations as low as 0.25 mg ml−1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The concentration dependence of the α-β transition temperature between 0.25 and 10 mg ml−1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same concentration range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.
publishDate 2016
dc.date.none.fl_str_mv 2016-09
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/11336/111213
Schwaighofer, Andreas; Alcaraz, Mirta Raquel; Araman, Can ; Goicoechea, Hector Casimiro; Lendl, Bernhard; External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations; Nature Publishing Group; Scientific Reports; 6; 9-2016; 33556-33566
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/111213
identifier_str_mv Schwaighofer, Andreas; Alcaraz, Mirta Raquel; Araman, Can ; Goicoechea, Hector Casimiro; Lendl, Bernhard; External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations; Nature Publishing Group; Scientific Reports; 6; 9-2016; 33556-33566
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.nature.com/articles/srep33556
info:eu-repo/semantics/altIdentifier/doi/10.1038/srep33556
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
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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 13.13397

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