Analysis of a 0.1-μm stepping bi-axis piezoelectric stage using a 2-DOF lumped model

Piezoelectric stages are widely used for parts manipulation, including micro-component assembly and bio-cell manipulation. This paper proposes a bi-axis piezoelectric stage based on a friction driven mechanism. The carrier slides on a supporting frame and slider constructed in the same plane as a low-profile stage. The dynamic model of the friction driven is based on a 2-DOF lumped model considering the impact and separation behavior. The first mass is the bulk piezoelectric actuator (slab)—as a vibrator—and the second is the driven slider. The stiffness ratio of the piezoelectric slab-to-the driven slider affects the output force of the slider because of the contact time ratio. Moreover, the stepping size is adjusted according to the duty ratio of the pulse width of the driving signal. The stepping size of 0.1 μm is achieved in the X and Y axes corresponding to 3% and 5% of the duty ratio, respectively, of 512-Hz carrier frequency in 20-Vpp driving signal. When the duty ratio is 100%, the full speed of 18 and 16 mm/s are achieved in the X- and Y-axes, respectively. The dimensions of the piezoelectric stage are 61 × 58 × 21.3 (high) mm³.

     

A Molecular Dynamics Simulation of the Human Lysozyme – Camelid VHH HL6 Antibody System

Amyloid diseases such as Alzheimer’s and thrombosis are characterized by an aberrant assembly of specific proteins or protein fragments into fibrils and plaques that are deposited in various tissues and organs. The single-domain fragment of a camelid antibody was reported to be able to combat against wild-type human lysozyme for inhibiting in-vitro aggregations of the amyloidogenic variant (D67H). The present study is aimed at elucidating the unbinding mechanics between the D67H lysozyme and VHH HL6 antibody fragment by using steered molecular dynamics (SMD) simulations on a nanosecond scale with different pulling velocities. The results of the simulation indicated that stretching forces of more than two nano Newton (nN) were required to dissociate the proteinantibody system, and the hydrogen bond dissociation pathways were computed.     

Target Molecular Simulations of RecA Family Protein Filaments

Modeling of the RadA family mechanism is crucial to understanding the DNA SOS repair process. In a 2007 report, the archaeal RadA proteins function as rotary motors (linker region: I71-K88) such as shown in Figure 1. Molecular simulations approaches help to shed further light onto this phenomenon. We find 11 rotary residues (R72, T75-K81, M84, V86 and K87) and five zero rotary residues (I71, K74, E82, R83 and K88) in the simulations. Inclusion of our simulations may help to understand the RadA family mechanism.