Time-resolved crystallography of ion pumping rhodopsins - Przemslaw Nogly (ETH Zurich, SWITZERLAND)
Автор: CCP4
Загружено: 2022-01-16
Просмотров: 285
Описание:
Ion pumping microbial rhodopsins are integral membrane proteins employing a common 7-transmembrane helices architecture to transport different ion types. The specific residue composition impacts the protein dynamics and transport mechanism.
Rhodopsins utilize retinal chromophore to harvest light energy for protein activation, which makes them an ideal target for pump-probe experiments. We employ serial crystallography to capture structural intermediates in “real-time” and at non-cryogenic temperatures. I will present a combination of the X-ray Free Electron Laser and more accessible synchrotron data, which provide complementary insights into protein dynamics and ion transport.
1. Weinert T et al., Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography (2019) Science 365, 61-65.
2. Nogly P et al., Retinal isomerization in bacteriorhodopsin captured by a femtosecond X-ray laser (2018) Science 361, 6398.
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