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dc.contributor.author
Alcaraz, Mirta Raquel
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dc.contributor.author
Schwaighofer, Andreas
dc.contributor.author
Goicoechea, Hector Casimiro
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dc.contributor.author
Lendl, Bernhard
dc.date.available
2019-01-30T19:18:21Z
dc.date.issued
2016-06
dc.identifier.citation
Alcaraz, Mirta Raquel; Schwaighofer, Andreas; Goicoechea, Hector Casimiro; Lendl, Bernhard; EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin; Springer Heidelberg; Analytical and Bioanalytical Chemistry; 408; 15; 6-2016; 3933-3941
dc.identifier.issn
1618-2642
dc.identifier.uri
http://hdl.handle.net/11336/69059
dc.description.abstract
In this work, a novel EC-QCL-based setup for mid-IR transmission measurements in the amide I region is introduced for monitoring dynamic changes in secondary structure of proteins. For this purpose, α-chymotrypsin (aCT) acts as a model protein, which gradually forms intermolecular β-sheet aggregates after adopting a non-native α-helical structure induced by exposure to 50 % TFE. In order to showcase the versatility of the presented setup, the effects of varying pH values and protein concentration on the rate of β-aggregation were studied. The influence of the pH value on the initial reaction rate was studied in the range of pH 5.8-8.2. Results indicate an increased aggregation rate at elevated pH values. Furthermore, the widely accessible concentration range of the laser-based IR transmission setup was utilized to investigate β-aggregation across a concentration range of 5-60 mg mL(-1). For concentrations lower than 20 mg mL(-1), the aggregation rate appears to be independent of concentration. At higher values, the reaction rate increases linearly with protein concentration. Extended MCR-ALS was employed to obtain pure spectral and concentration profiles of the temporal transition between α-helices and intermolecular β-sheets. Comparison of the global solutions obtained by the modelled data with results acquired by the laser-based IR transmission setup at different conditions shows excellent agreement. This demonstrates the potential and versatility of the EC-QCL-based IR transmission setup to monitor dynamic changes of protein secondary structure in aqueous solution at varying conditions and across a wide concentration range. Graphical abstract EC-QCL IR spectroscopy for monitoring protein conformation change.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer Heidelberg
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
2,2,2-Trifluoroethanol
dc.subject
Aggregation
dc.subject
Infrared Spectroscopy
dc.subject
Multivariate Curve Resolution-Alternating Least Squares
dc.subject
Protein Secondary Structure
dc.subject
Quantum Cascade Laser
dc.subject.classification
Otras Ciencias Químicas
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dc.subject.classification
Ciencias Químicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
EC-QCL mid-IR transmission spectroscopy for monitoring dynamic changes of protein secondary structure in aqueous solution on the example of β-aggregation in alcohol-denaturated α-chymotrypsin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-22T18:51:22Z
dc.identifier.eissn
1618-2650
dc.journal.volume
408
dc.journal.number
15
dc.journal.pagination
3933-3941
dc.journal.pais
Alemania
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dc.journal.ciudad
Heidelberg
dc.description.fil
Fil: Alcaraz, Mirta Raquel. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Vienna University of Technology; Austria
dc.description.fil
Fil: Schwaighofer, Andreas. Vienna University of Technology; Austria
dc.description.fil
Fil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
dc.description.fil
Fil: Lendl, Bernhard. Vienna University of Technology; Austria
dc.journal.title
Analytical and Bioanalytical Chemistry
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00216-016-9464-5
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00216-016-9464-5
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