<div class="csl-bib-body">
<div class="csl-entry">Lendl, B., Alcaráz, M. R., Schwaighofer, A., & Goicoechea, H. (2016). 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. <i>Analytical and Bioanalytical Chemistry</i>, <i>408</i>, 3933–3941. https://doi.org/10.1007/s00216-016-9464-5</div>
</div>
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dc.identifier.issn
1618-2642
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/18
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dc.description
The final publication is available at Springer via <a href="https://doi.org/10.1007/s00216-016-9464-5" target="_blank">https://doi.org/10.1007/s00216-016-9464-5</a>.
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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.
en
dc.description.sponsorship
Agilent Technologies University Relations Grant
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dc.description.sponsorship
Austrian research fundingassociation (FFG)
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dc.language
English
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dc.language.iso
en
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dc.publisher
SPRINGER NATURE
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dc.relation.ispartof
Analytical and Bioanalytical Chemistry
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dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
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dc.subject
Quantum cascade laser
en
dc.subject
Infrared spectroscopy
en
dc.subject
Multivariate curve resolution-alternating
en
dc.subject
least squares
en
dc.subject
Protein secondary structure
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dc.subject
Aggregation
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dc.subject
2,2,2-Trifluoroethanol
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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
en
dc.type
Article
en
dc.type
Artikel
de
dc.rights.license
Creative Commons Namensnennung 4.0 International
de
dc.rights.license
Creative Commons Attribution 4.0 International
en
dc.contributor.affiliation
Universidad Nacional del Litoral, Argentina
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dc.description.startpage
3933
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dc.description.endpage
3941
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dc.relation.grantno
3375
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dc.relation.grantno
imPACts 843546
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dc.rights.holder
The Author(s) 2016
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dc.type.category
Original Research Article
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tuw.container.volume
408
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tuw.journal.peerreviewed
true
-
tuw.peerreviewed
true
-
tuw.version
vor
-
wb.publication.intCoWork
International Co-publication
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dcterms.isPartOf.title
Analytical and Bioanalytical Chemistry
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tuw.publication.orgunit
E164 - Institut für Chemische Technologien und Analytik
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tuw.publisher.doi
10.1007/s00216-016-9464-5
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dc.identifier.eissn
1618-2650
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dc.identifier.libraryid
AC11360101
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dc.description.numberOfPages
9
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dc.identifier.urn
urn:nbn:at:at-ubtuw:3-1668
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tuw.author.orcid
0000-0003-3838-5842
-
tuw.author.orcid
0000-0003-2714-7056
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tuw.author.orcid
0000-0001-7145-0082
-
dc.rights.identifier
CC BY 4.0
de
dc.rights.identifier
CC BY 4.0
en
item.languageiso639-1
en
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item.cerifentitytype
Publications
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Publications
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http://purl.org/coar/resource_type/c_18cf
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item.openairecristype
http://purl.org/coar/resource_type/c_18cf
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item.fulltext
with Fulltext
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item.openaccessfulltext
Open Access
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item.grantfulltext
open
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item.openairetype
Article
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item.openairetype
Artikel
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crisitem.author.dept
E164-02 - Forschungsbereich Umwelt-, Prozessanalytik und Sensoren
-
crisitem.author.dept
E164 - Institut für Chemische Technologien und Analytik
-
crisitem.author.dept
E164-02-1 - Forschungsgruppe Prozessanalytik
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crisitem.author.dept
Universidad Nacional del Litoral, Argentina
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crisitem.author.orcid
0000-0003-3838-5842
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crisitem.author.orcid
0000-0003-2714-7056
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crisitem.author.orcid
0000-0001-7145-0082
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crisitem.author.parentorg
E164 - Institut für Chemische Technologien und Analytik
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crisitem.author.parentorg
E150 - Fakultät für Technische Chemie
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crisitem.author.parentorg
E164-02 - Forschungsbereich Umwelt-, Prozessanalytik und Sensoren