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RESEARCH PRODUCT
Conformational dynamics of a single protein monitored for 24 hours at video rate
Christoph RatzkeWeixiang YeCarsten SönnichsenJanak PrasadRubén Ahijado-guzmánLaura TütingJulia RickenThorsten HugelSirin CeliksoyMarkus GötzSeraphine V. Wegnersubject
0301 basic medicineLetterProtein ConformationMolecular ConformationFOS: Physical sciencesHsp90Bioengineeringsingle molecule02 engineering and technology7. Clean energyQuantitative Biology - Quantitative Methods03 medical and health sciencesMolecular dynamicsFluorescence Resonance Energy TransferNanotechnologyGeneral Materials ScienceHSP90 Heat-Shock ProteinsPhysics - Biological PhysicsQuantitative Methods (q-bio.QM)PlasmonPhysicsVideo rateMechanical EngineeringProtein dynamics92Biomolecules (q-bio.BM)General ChemistrySurface Plasmon Resonance021001 nanoscience & nanotechnologyCondensed Matter PhysicsGold nanospheres030104 developmental biologyFörster resonance energy transferQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)Chemical physicsFOS: Biological sciencesprotein dynamicsPlasmon rulernonergodicityGold0210 nano-technologyLinkerdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2018-01-01 |