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Right here, we control MTBD either in high-affinity or low-affinity states by presenting a disulfide bond to your stalk and analyze the ensuing structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding regarding the stalk α-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk α-helix even without the disulfide relationship, sugg
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