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High-Speed Atomic Force Microscopy: A Novel Tool to Study Structure and Dynamics of Single Unlabeled Membrane Proteins

The advent of high-speed atomic force microscopy (HS-AFM(1)) has opened a novel research field for the dynamic analysis of single bio-molecules: Molecular motor dynamics (2,3), membrane protein diffusion (4), assembly (5) and conformational changes (6) could be directly visualized. Further developments for buffer exchange (7) and temperature control (8) during HS-AFM operation provide breakthroughs towards the performance of dynamic structural biochemistry using HS-AFM. I will exemplify the power of HS-AFM for the quantitative analysis of function-related structural dynamics on the membrane deformation complex ESCRT-III (5), a glutamate transporter homologue (6), and ligand-gated ion channels (9,10). Finally, I will introduce high-speed AFM line scanning (HS-AFM-LS) and high-speed AFM height spectroscopy (HS-AFM-HS) that reaches millisecond and microsecond temporal resolution of single molecule dynamics (11). 


1) Ando, Chem Rev 2014, 114(6):3120-88

2) Kodera, Nature 2010, 468(7320):72-6

3) Uchihashi, Science 2011, 333(6043):755-8

4) Casuso, Nat Nanotechnol 2012, 7(8):525-9

5) Chiaruttini, Cell 2015, 163(4):866-79.

6) Ruan, PNAS 2017, 114(7):1584-1588

7) Miyagi, Nat Nanotechnol 2016, 11(9):783-90

8) Takahashi, Small 2016, 12(44):6106-6113

9) Ruan, 2018 115(41):10333-10338

10) Marchesi, Nature Communications, 2018, 9(1):3978

11) Heath and Scheuring, Nature Communications, 2018, 9(1):4983

La conférence est pour tout public et le café est servi dès 11h30.


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