Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization
Vibrational dynamics of the retinal all-trans to 13-cis photoisomerization in channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) was investigated by femtosecond visible pump mid-IR probe spectroscopy. After photoexcitation, the transient infrared absorption of C-C stretching modes was detected....
Main Authors: | T. Stensitzki, Y. Yang, V. Muders, R. Schlesinger, J. Heberle, K. Heyne |
---|---|
Format: | Article |
Language: | English |
Published: |
AIP Publishing LLC and ACA
2016-07-01
|
Series: | Structural Dynamics |
Online Access: | http://dx.doi.org/10.1063/1.4948338 |
Similar Items
-
The primary photoreaction of channelrhodopsin-1: Wavelength dependent photoreactions induced by ground-state heterogeneity
by: Karsten eHeyne, et al.
Published: (2015-07-01) -
Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump—IR-Probe Spectroscopy and Computational Methods
by: Till Stensitzki, et al.
Published: (2020-02-01) -
Vibronic dynamics of the ultrafast all-trans to 13-cis photoisomerization of retinal in channelrhodopsin-1
by: Schnedermann, C, et al.
Published: (2016) -
Atomistic Insight into the Role of Threonine 127 in the Functional Mechanism of Channelrhodopsin-2
by: David Ehrenberg, et al.
Published: (2019-11-01) -
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin
by: Kazumasa Oda, et al.
Published: (2021-03-01)