pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy

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dc.identifier.uri http://dx.doi.org/10.15488/5102
dc.identifier.uri https://www.repo.uni-hannover.de/handle/123456789/5146
dc.contributor.author Kniggendorf, Ann-Kathrin
dc.contributor.author Schmidt, David
dc.contributor.author Roth, Bernhard
dc.contributor.author Plettenburg, Oliver
dc.contributor.author Zeilinger, Carsten
dc.date.accessioned 2019-07-04T11:37:33Z
dc.date.available 2019-07-04T11:37:33Z
dc.date.issued 2019
dc.identifier.citation Kniggendorf, A.-K.; Schmidt, D.; Roth, B.; Plettenburg, O.; Zeilinger, C.: pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy. In: International Journal of Molecular Sciences 20 (2019), Nr. 11, 2736. DOI: https://doi.org/10.3390/ijms20112736
dc.description.abstract KcsA is a tetrameric potassium channel formed out of four identical monomeric subunits used as a standard model for selective potassium transport and pH-dependent gating. Large conformational changes are reported for tetramer and monomer upon gating, and the response of the monomer being controversial with the two major studies partially contradicting each other. KcsA was analyzed as functional tetramers embedded in liposomes and as monomer subunits with confocal Raman microscopy under physiological conditions for the active and the closed channel state, using 532 nm excitation to avoid introducing conformational changes during the measurement. Channel function was confirmed using liposome flux assay. While the classic fingerprint region below 1800 rel. cm-1 in the Raman spectrum of the tetramer was unaffected, the CH-stretching region between 2800 and 3200 rel. cm-1 was found to be strongly affected by the conformation. No pH-dependency was observed in the Raman spectra of the monomer subunits, which closely resembled the Raman spectrum of the tetramer in its active conformation, indicating that the open conformation of the monomer and not the closed conformation as postulated may equal the relaxed state of the molecule. eng
dc.language.iso eng
dc.publisher Basel : MDPI AG
dc.relation.ispartofseries International Journal of Molecular Sciences 20 (2019), Nr. 11
dc.rights CC BY 4.0
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject 532 nm eng
dc.subject KcsA eng
dc.subject liposome flux assay eng
dc.subject monomer eng
dc.subject pH-dependent gating eng
dc.subject Raman spectroscopy eng
dc.subject tetramer eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.subject.ddc 540 | Chemie ger
dc.title pH-Dependent Conformational Changes of KcsA Tetramer and Monomer Probed by Raman Spectroscopy
dc.type article
dc.type Text
dc.relation.issn 1422-0067
dc.relation.doi https://doi.org/10.3390/ijms20112736
dc.bibliographicCitation.issue 11
dc.bibliographicCitation.volume 20
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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