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rob.mechanochemistry.org

@rob.mechanochemistry.org
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rob.mechanochemistry.org @rob.mechanochemistry.org · 11/07/2026
In www.biorxiv.org/content/10.6... Yean Ming Chew & I show that mutating the interPF interface in human MTs can allow them to assemble in GDP. We propose that tubulin molecules are captured indiscriminately at MT tips but then retained only if they can bind stably to a lateral nearest-neighbour.
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rob.mechanochemistry.org @rob.mechanochemistry.org · 18/02/2026
After trenchant reviewing, Karnawat et al is out, showing that ATPγS causes single kinesin molecules to pause under load in an Await-Isomerisation (AI) state that leaks hand-over-hand backsteps. In ATP we think this state serves to couple forward stepping to hydrolysis www.nature.com/articles/s41...
nature.com
ATPγS substantially defeats the biasing mechanism for kinesin steps - Nature Communications
ATPγS, a slowly-hydrolysed ATP analogue, causes kinesin to take extra backsteps under load. Here, the authors examine single-molecule mechanics and propose a state in which forward steps and coupled A...
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rob.mechanochemistry.org @rob.mechanochemistry.org · 04/12/2025
Have to feel for the grey eduWOSM. It's just so .. grey ..
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rob.mechanochemistry.org @rob.mechanochemistry.org · 22/06/2025
Nick showing Ron Vale the eduWOSM.
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rob.mechanochemistry.org @rob.mechanochemistry.org · 02/05/2025
In BIORXIV/2025/651652, we use ATPγS to reveal a previously-occult kinesin state. In the Await-Isomerisation (AI) state, ATP is bound but NL docking and hydrolysis are inhibited. ATPγS overstabilises the AI state, producing a characteristic signature of load-independent 8 nm tethered backslips:
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rob.mechanochemistry.org @rob.mechanochemistry.org · 05/04/2025
Nick has been in Rennes, helping Romain Gibeaux install a WOSM-TIRF. Big happiness!
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rob.mechanochemistry.org @rob.mechanochemistry.org · 14/03/2025
Prakash et al (doi.org/10.1101/2025...), emerging from a happy & ongoing multilab collaboration, shows that a mix of human α1β3 and α1β4 tubulins assembles in vitro into segmented microtubules in which the segments have different protofilament numbers, and are recognized by different MAPS.
doi.org
Tubulin isotypes polymerise into sectioned microtubules that locally regulate protein binding
Microtubules assemble from tubulin heterodimers composed of conserved α- and β- tubulins. In many species, including humans, tubulins are expressed from multiple genes. While the resulting tubulin iso...
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rob.mechanochemistry.org @rob.mechanochemistry.org · 12/02/2025
Yean Ming Chew and I wrote doi.org/10.1042/BST2... about MT lattice switching. We discuss evidence that protofilament-level structural switching is ancient and fundamental and conserved; and that tubulation creates new allosteric interfaces that operate on essentially the same structural switch.
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