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Biomolecular dynamics studied with IR-spectroscopy using quantum cascade lasers combined with nanosecond perturbation techniques

Biomolecular dynamics studied with IR-spectroscopy using quantum cascade lasers combined with nanosecond perturbation techniques

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POPP, Alexander, David SCHEERER, Benjamin Stefan HECK, Karin HAUSER, 2017. Biomolecular dynamics studied with IR-spectroscopy using quantum cascade lasers combined with nanosecond perturbation techniques. In: Spectrochimica Acta / Part A: Molecular and Biomolecular Spectroscopy. 181, pp. 192-199. ISSN 1386-1425. eISSN 1873-3557

@article{Popp2017-06Biomo-39285, title={Biomolecular dynamics studied with IR-spectroscopy using quantum cascade lasers combined with nanosecond perturbation techniques}, year={2017}, doi={10.1016/j.saa.2017.03.053}, volume={181}, issn={1386-1425}, journal={Spectrochimica Acta / Part A: Molecular and Biomolecular Spectroscopy}, pages={192--199}, author={Popp, Alexander and Scheerer, David and Heck, Benjamin Stefan and Hauser, Karin} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/39285"> <dcterms:issued>2017-06</dcterms:issued> <dc:contributor>Popp, Alexander</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-06-14T10:00:06Z</dcterms:available> <dc:contributor>Heck, Benjamin Stefan</dc:contributor> <dc:contributor>Scheerer, David</dc:contributor> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/39285"/> <dcterms:abstract xml:lang="eng">Early events of protein folding can be studied with fast perturbation techniques triggering non-equilibrium relaxation dynamics. A nanosecond laser-excited pH-jump or temperature-jump (T-jump) was applied to initiate helix folding or unfolding of poly-l-glutamic acid (PGA). PGA is a homopolypeptide with titratable carboxyl side-chains whose protonation degree determines the PGA conformation. A pH-jump was realized by the photochemical release of protons and induces PGA folding due to protonation of the side-chains. Otherwise, the helical conformation can be unfolded by a T-jump. We operated under conditions where PGA does not aggregate and temperature and pH are the regulatory properties of its conformation. The experiments were performed in such a manner that the folding/unfolding jump proceeded to the same PGA conformation. We quantified the increase/decrease in helicity induced by the pH-/T-jump and demonstrated that the T-jump results in a relatively small change in helical content in contrast to the pH-jump. This is caused by the strong pH-dependence of the PGA conformation. The conformational changes were detected by time-resolved single wavelength IR-spectroscopy using quantum cascade lasers (QCL). We could independently observe the kinetics for α-helix folding and unfolding in PGA by using different perturbation techniques and demonstrate the high sensitivity of time-resolved IR-spectroscopy to study protein folding mechanisms.</dcterms:abstract> <dc:creator>Heck, Benjamin Stefan</dc:creator> <dcterms:title>Biomolecular dynamics studied with IR-spectroscopy using quantum cascade lasers combined with nanosecond perturbation techniques</dcterms:title> <dc:creator>Hauser, Karin</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-06-14T10:00:06Z</dc:date> <dc:language>eng</dc:language> <dc:creator>Popp, Alexander</dc:creator> <dc:creator>Scheerer, David</dc:creator> <dc:contributor>Hauser, Karin</dc:contributor> </rdf:Description> </rdf:RDF>

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