Temperature-sensitive gating of hCx26

High-resolution Raman spectroscopy sheds light on conformational changes

Verfasst von

Ann Kathrin Kniggendorf, Merve Meinhardt-Wollweber, Xiaogang Yuan, Bernhard Roth, Astrid Seifert, Niels Fertig, Carsten Zeilinger

Abstract

The temperature-sensitive gating of human Connexin 26 (hCx26) was analyzed with confocal Raman microscopy. High-resolution Raman spectra covering the spectral range between 400 and 1500 rel. cm−1 with a spectral resolution of 1 cm−1 were fully annotated, revealing notable differences between the spectrum recorded from solubilized hCx26 in Ca2+-buffered POPC at 10°C and any other set of protein conditions (temperature, Ca2+ presence, POPC presence). Spectral components originating from specific amino acids show that the TM1/EL1 parahelix and probably the TM4 trans-membrane helix and the plug domain are involved in the gating process responsible for fully closing the hemichannel.

Details

Organisationseinheit(en): Hannoversches Zentrum für Optische Technologien (HOT)
Abteilung Zellphysiologie und Biophysik
Zentrum für Biomolekulare Wirkstoffe (BMWZ)
Externe Organisation(en): Nanion Technologies GmbH
Exzellenzcluster Hearing4all
Typ: Artikel
Journal: Biomedical optics express
Band: 5
Seiten: 2054-2065
Anzahl der Seiten: 12
ISSN: 2156-7085
Publikationsdatum: 01.06.2014
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Biotechnologie, Atom- und Molekularphysik sowie Optik
Elektronische Version(en): https://doi.org/10.1364/BOE.5.002054 (Zugang: Offen )

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