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Updated: Feb 6, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
Published on: March 21, 2025
A revisit of the conformational dynamics of SNARE protein rYkt6
Shaowen Wu1, Dongdong Wang1, Jingwei Weng1
1Multiscale Research Institute of Complex Systems, Department of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai, PR China.
Abstract:
N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are involved in the fusion of vesicles with their target membranes. R-SNARE protein Ykt6 is one of the most conserved SNARE in eukaryotes. The conformational state of Ykt6 is regulated by the lipidations at its C-terminal motif. Previous studies show that the binding of dodecylphosphocholine (DPC) can stabilize a closed conformation of rat Ykt6 (rYkt6) and mimic the farnesylated rYkt6. Despite this model, the detailed conformational dynamics of Ykt6 is still unclear. Here, we combined smFRET and MD simulation to demonstrate that the un-lipidated rYkt6 adopts five major conformational states. DPC binding shifts the conformational distribution toward the more closed states. At the same time, there remain considerable fractions of open and semi-open conformations in the presence of DPC. These newly revealed dynamic features of rYkt6 are consistent with its unique functional diversity in neuronal cells.
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