Design of a Hierarchical Assembly at a Solid-Liquid Interface Using an Asymmetric Protein Needle.

Design and control of processes for a hierarchical assembly of proteins remain challenging because it requires consideration of design principles with atomic-level accuracy. Previous studies have adopted symmetry-based strategies to minimize the complexity of protein-protein interactions and this has placed constraints on the structures of the resulting protein assemblies. In the present work, we used an anisotropic-shaped protein needle, gene product 5 (gp5) from bacteriophage T4 with a C-terminal hexahistidine-tag (His-tag) (gp5_CHis), to construct a hierarchical assembly with two distinct protein-protein interaction sites.

Protein Needles Designed to Self-Assemble through Needle Tip Engineering.

The dynamic process of formation of protein assemblies is essential to form highly ordered structures in biological systems. Advances in structural and synthetic biology have led to the construction of artificial protein assemblies. However, development of design strategies exploiting the anisotropic shape of building blocks of protein assemblies has not yet been achieved.

Development of Low-Frequency Phased Array for Imaging Defects in Concrete Structures.

The nondestructive inspection of concrete structures is indispensable for ensuring the safety and reliability of aging infrastructures. Ultrasonic waves having a frequency of tens of kHz are frequently used to reduce the scattering attenuation due to coarse aggregates. Such low frequencies enable the measurement of the thickness of concrete structures and detection of layer-type defects, such as delamination, whereas it causes a lack of sensitivity to crack-type defects.

The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design.

Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens. Such subunit vaccines are much safer than traditional vaccines based on inactivated pathogens which are more likely to produce side-effects.

Dynamic behavior of an artificial protein needle contacting a membrane observed by high-speed atomic force microscopy.

Bacteriophage T4 and other bacteriophages have a protein component known as a molecular needle which is used for the transmembrane reaction in the infection process. In this paper, the transmembrane reaction mechanisms of artificial protein needles (PNs) constructed by protein engineering of the component protein of bacteriophage T4 are elucidated by observation of single-molecules by high-speed atomic force microscopy (HS-AFM) and molecular dynamics (MD) simulations. The HS-AFM images indicate that the tip of the needle structure stabilizes the interaction of the needle with the membrane surface and is involved in controlling the contact angle and angular velocity with respect to the membrane.