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A micro-electromechanical resonator, consisting of a $$125 \times 125\,\upmu \hbox {m}^2$$ center plate suspended $$2\,\upmu \hbox {m}$$ above a substrate, was immersed in $$^4$$ He along with a quartz tuning fork. The tuning fork was placed 5 mm above the resonator and was used to generate turbulence. The damping of the resonator was investigated in the presence of turbulence generated by the tuning fork. We observe a velocity, $$v_c \simeq 5\,\hbox {mm}\,\hbox {s}^{-1}$$ , above which the damping on the resonator is drastically reduced for all tuning fork velocities studied. We attribute this change in damping to the shedding and capture of vortices.

Whole-exome sequencing of samples from affected members of two unrelated families with late-onset non-syndromic hearing loss revealed a novel mutation (c.2090 T > G; NM_017433) in MYO3A. The mutation was confirmed in 36 affected individuals, showing autosomal dominant inheritance. The mutation alters a single residue (L697W or p.Leu697Trp) in the motor domain of the stereocilia protein MYO3A, leading to a reduction in ATPase activity, motility, and an increase in actin affinity. MYO3A-L697W showed reduced filopodial actin protrusion initiation in COS7 cells, and a predominant tipward accumulation at filopodia and stereocilia when coexpressed with wild-type MYO3A and espin-1, an actin-regulatory MYO3A cargo. The combined higher actin affinity and duty ratio of the mutant myosin cause increased retention time at stereocilia tips, resulting in the displacement of the wild-type MYO3A protein, which may impact cargo transport, stereocilia length, and mechanotransduction. The dominant negative effect of the altered myosin function explains the dominant inheritance of deafness.

Myosin 5c (Myo5c) is a low duty ratio, non-processive motor unable to move continuously along actin filaments though it is believed to participate in secretory vesicle trafficking in vertebrate cells. Here, we measured the ATPase kinetics of Myo5c dimers and tested the possibility that the coupling of two Myo5c molecules enables processive movement. Steady-state ATPase activity and ADP dissociation kinetics demonstrated that a dimer of Myo5c-HMM (double-headed heavy meromyosin 5c) has a 6-fold lower Km for actin filaments than Myo5c-S1 (single-headed myosin 5c subfragment-1), indicating that the two heads of Myo5c-HMM increase F-actin-binding affinity. Nanometer-precision tracking analyses showed that two Myo5c-HMM dimers linked with each other via a DNA scaffold and moved processively along actin filaments. Moreover, the distance between the Myo5c molecules on the DNA scaffold is an important factor for the processive movement. Individual Myo5c molecules in two-dimer complexes move stochastically in 30–36 nm steps. These results demonstrate that two dimers of Myo5c molecules on a DNA scaffold increased the probability of rebinding to F-actin and enabled processive steps along actin filaments, which could be used for collective cargo transport in cells.

An acidimetric procedure for the determination of glycerol following oxidation with periodic acid has been described. This procedure has been successfully applied to C. P. grade glycerin, spent soap lyes, soap lye crudes, half crudes, saponification crudes, evaporator salt, and mixtures of glycerol with trimethylene glycol and polyglycerols. Factors that influence the determination, such as size of sample, presence of salt and the presence of organic compounds containing hydroxyl groups, have been discussed.