Conformational Dynamics of a Single Protein Monitored
for 24 h at Video Rate
Version 3 2018-10-10, 23:48
Version 2 2018-09-25, 13:52
Version 1 2018-09-25, 13:46
Posted on 2018-10-10 - 23:48
We
use plasmon rulers to follow the conformational dynamics of
a single protein for up to 24 h at a video rate. The plasmon ruler
consists of two gold nanospheres connected by a single protein linker.
In our experiment, we follow the dynamics of the molecular chaperone
heat shock protein 90 (Hsp90), which is known to show “open”
and “closed” conformations. Our measurements confirm
the previously known conformational dynamics with transition times
in the second to minute time scale and reveals new dynamics on the
time scale of minutes to hours. Plasmon rulers thus extend the observation
bandwidth 3–4 orders of magnitude with respect to single-molecule
fluorescence resonance energy transfer and enable the study of molecular
dynamics with unprecedented precision.
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Ye, Weixiang; Götz, Markus; Celiksoy, Sirin; Tüting, Laura; Ratzke, Christoph; Prasad, Janak; et al. (2018). Conformational Dynamics of a Single Protein Monitored
for 24 h at Video Rate. ACS Publications. Collection. https://doi.org/10.1021/acs.nanolett.8b03342
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AUTHORS (11)
WY
Weixiang Ye
MG
Markus Götz
SC
Sirin Celiksoy
LT
Laura Tüting
CR
Christoph Ratzke
JP
Janak Prasad
JR
Julia Ricken
SW
Seraphine V. Wegner
RA
Rubén Ahijado-Guzmán
TH
Thorsten Hugel
CS
Carsten Sönnichsen