Protein engineering: Construction of Robust Bio‐nanotubes using the Controlled Self‐Assembly of Component Proteins of Bacteriophage T4 (Small 17/2010)

The cover image shows a designed bio-nanotube made by the fusion of different component proteins of bacteriophage T4. The locations and structures of the original proteins, foldon, and β-helix of bacteriophage T4 are highlighted by the inset images. The crystal structure of the bio-nanotube shows that it has a well-defined length of 10 nm as a result of head-tohead dimerization when the β-helical proteins are capped with the foldon, which serves as a nucleation site for helical structures. Surprisingly, the tube assembly has high thermal stability (∼100 °C), tolerance to organic solvents, and a wide pH stability range of pH 2–10. These insights are expected to contribute to the development of intriguing strategies for the preparation of new bio-architectures for nano/mesoscale materials applications. For more information, please read the Communication “Construction of Robust Bio-nanotubes using the Controlled Self-Assembly of Component Proteins of Bacteriophege T4” by T. Ueno and co-workers, beginning on page 1873.