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 -