Temperature-sensitive gating of hCx26: high-resolution Raman spectroscopy sheds light on conformational changes.
Temperature-sensitive gating of hCx26: high-resolution Raman spectroscopy sheds light on conformational changes.
复制标题
hCx26 的温度敏感门控：高分辨率拉曼光谱揭示构象变化。
DOI：
--
复制
发表时间：
2014
影响因子：
3.4
通讯作者：
C. Zeilinger
中科院分区：
文献类型：
--
作者：
A. Kniggendorf;M. Meinhardt;Xiao;B. Roth;A. Seifert;N. Fertig;C. Zeilinger
用共聚焦拉曼显微镜分析了人连接蛋白26 （Connexin 26, hCx26）的温度敏感门控。高分辨率拉曼光谱覆盖400 - 1500 rel. cm（-1）的光谱范围，光谱分辨率为1 cm(-1)，显示了溶解hCx26在Ca（2+）缓冲的POPC中在10°C下记录的光谱与任何其他蛋白质条件（温度，Ca（2+）存在，POPC存在）之间的显着差异。来自特定氨基酸的光谱成分表明，TM1/EL1副螺旋，可能还有TM4跨膜螺旋和塞结构域参与了负责完全关闭半通道的门通过程。
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 Ca(2+)-buffered POPC at 10°C and any other set of protein conditions (temperature, Ca(2+) 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.
DOI：
10.1021/jz101619f
发表时间：
2011-02-17
期刊：
The journal of physical chemistry letters
影响因子：
--
作者：
Oladepo SA;Xiong K;Hong Z;Asher SA
通讯作者：
Asher SA