RT Journal Article
T1 Conformational dynamics of a single protein monitored for 24 h at video rate
A1 Ye, Weixiang
A1 Götz, Markus
A1 Celiksoy, Sirin
A1 Tüting, Laura
A1 Ratzke, Christoph
A1 Prasad, Janak
A1 Ricken, Julia
A1 Wegner, Seraphine
A1 Ahijado Guzmán, Rubén
A1 Hugel, Thorsten
A1 Sönnichsen, Carsten
AB 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.
PB American Chemical Society
SN 1530-6984
YR 2018
FD 2018
LK https://hdl.handle.net/20.500.14352/93208
UL https://hdl.handle.net/20.500.14352/93208
LA eng
NO Ye, W.; Götz, M.; Celiksoy, S.; Tüting, L.; Ratzke, C.; Prasad, J.; Ricken, J.; Wegner, S. V.; Ahijado-Guzmán, R.; Hugel, T.; Sönnichsen, C. Conformational Dynamics of a Single Protein Monitored for 24 h at Video Rate. Nano Lett. 2018, 18, 6633-6637 DOI:10.1021/acs.nanolett.8b03342.
NO European Commission
DS Docta Complutense
RD 18 abr 2025