Details
| Original language | English |
|---|---|
| Pages (from-to) | 2054-2065 |
| Number of pages | 12 |
| Journal | Biomedical optics express |
| Volume | 5 |
| Issue number | 7 |
| Publication status | Published - 1 Jun 2014 |
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.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Physics and Astronomy(all)
- Atomic and Molecular Physics, and Optics
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In: Biomedical optics express, Vol. 5, No. 7, 01.06.2014, p. 2054-2065.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Temperature-sensitive gating of hCx26
T2 - High-resolution Raman spectroscopy sheds light on conformational changes
AU - Kniggendorf, Ann Kathrin
AU - Meinhardt-Wollweber, Merve
AU - Yuan, Xiaogang
AU - Roth, Bernhard
AU - Seifert, Astrid
AU - Fertig, Niels
AU - Zeilinger, Carsten
PY - 2014/6/1
Y1 - 2014/6/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84903725244&partnerID=8YFLogxK
U2 - 10.1364/BOE.5.002054
DO - 10.1364/BOE.5.002054
M3 - Article
AN - SCOPUS:84903725244
VL - 5
SP - 2054
EP - 2065
JO - Biomedical optics express
JF - Biomedical optics express
SN - 2156-7085
IS - 7
ER -