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See how a AAA machine uses stochasticity to promote fast protein translocation:
youtu.be/J5An-TBEjZk
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Check the paper describing these findings here:
nature.com/articles/s41467-0…
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Our new paper shows that the AAA machine ClpB uses a stochastic, Brownian-ratchet like mechnism to translocate proteins in miliseconds.
nature.com/articles/s41467-0…
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Want to learn how single-molecule FRET can study the translocation of proteins by AAA machines (youtu.be/J5An-TBEjZk)?
Read this paper: biorxiv.org/content/10.1101/…
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Our newest paper uses single-molecule FRET to reveal how the AAA machine ClpB uses a Brownian-ratchet like mechanism to translocate proteins - taking milliseconds, depending weakly on temperature, and sometimes starting in the 'wrong' direction.
doi.org/10.1101/2025.03.13.6…
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New paper alert!
How do enzyme motions contribute to catalysis? Using single-molecule FRET, we uncovered how a denaturant enhances adenylate kinase activity—through controlling conformational dynamics and fine-tuning substrate binding!
Read more here: doi.org/10.1039/D4SC06819J
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Within a new Max Planck-Weizmann Institute collaboration, @SandoghdarLab and @HaranLab seek a joint postdoc to develop photon collection methods for single-molecule studies of microsecond protein dynamics. Write to: vahid.sandoghdar@mpl.mpg.de, gilad.haran@weizmann.ac.il.
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Single-moleucle FRET and NMR complement each other in studying very fast (microsecond) large-scale conformational transitions of proteins as they relate to function. In a new Annu. Rev. Biophys. paper with Paul Schanda, we discuss this complementarity.
shorturl.at/iCQ39
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Think you know everything about GroEL? Read this: each subunit of this molecular chaperone flucutates on the microsecond time scale between 4 conformational states, yet these fast fluctuations impact the much-slower function of the whole machine!
pubs.acs.org/doi/10.1021/acs…
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Have you wondered how fast (microsecond-millisecond) large-scale conformational dynamics of protein machines can affect their often-much-slower functional cycles? Read our new Perspective in JPC B to learn.
pubs.acs.org/doi/full/10.102…
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Have you wondered how the very rough surfaces of immune cells affect the lateral distribution of proteins? One way to study this is to combine super-resolution microscopy with variable-angle TIRF 3D membrane mapping- microvillar cartography. See:
link.springer.com/protocol/1…
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How can microsecond conformational changes affect an enzyme's much slower catalytic cycle? Our single-molecule study of substrate inhibition in adenylate kinase helps unlock this mystery. Have a look!
pnas.org/doi/10.1073/pnas.22…
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Our latest adventure into the workings of the disaggregation machine ClpB is on bioRxiv, demonstrating the elaborate allosteric wiring of the machine by single-molecule FRET and MD simulations.
biorxiv.org/content/10.1101/…
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Our new paper discusses the effect of experimental time resolution on the measurement of free-energy barrier-crossing events in protein folding reactions. I am a junior author together with three great theoreticians: Makarov, Berezhkovskii, and Pollak.
pubs.acs.org/doi/full/10.102…
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Want to learn about plasmonic cavities and their strong coupling to individual quantum dots? See our new Accounts of Chemical Research paper!
pubs.acs.org/doi/10.1021/acs…
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Our new review in The FEBS Journal, describing our single-molecule FRET studies of the disaggregation machine ClpB, is now online. Read about fast motions within this important machine and how they couple to its overall functional cycle.
doi.org/10.1111/febs.16539
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Check our new paper in which correlated motions of lipids in membranes are measured and shown to extend over hundreds of nanometers. The analysis of these correlations indicates that hydrodynamic theory is appropriate for predicting membrane dynamics.
pnas.org/content/118/48/e211…
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Our new study in Science Advances demonstrates that pore loops of the disaggregation machine ClpB demonstrate microsecond dynamics that correlate with activity, suggesting a Brownian ratchet mechanism for substrate threading.
science.org/doi/10.1126/scia…
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