Flagelliform silk proteins

Dicko, C., Knight, D., Kenney, J. M., and Vollrath, F. (2004b). Secondary structures and conformational changes in flagelliform, cylindrical, major, and minor ampullate silk proteins. Temperature and concentration effects. Biomacromolecules 5, 2105-2115. 

Zhou, Y. Wu, S. Conticello, V.P. Genetically directed synthesis and spectroscopic analysis of a protein polymer derived from a flagelliform silk sequence. Biomacromolecules 2 11K115 (2001). Zurovec, M. Sehnal, F. Unique molecular architecture of silk fibroin in the waxmoth. Galleria mellonella. J. Biol Chem. 111. 22639-22647 (2002). 

Hayashi, C.Y. Lewis, R.V. Spider flagelliform silk lessons in protein design, gene structure, and molecular evolution. Bioessays 23 750-756 (2001). 

Rising, A., Hjalm, G., Engstrom, W and Johansson, J. (2006). N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindri-form spider silk proteins. Biomacromolecules 7, 3120-3124. 

Conticello and co-workers (47) have also produced alternating block copolymers containing a flagelliform-like sequence (GPGQQ)e, which is derived from the A. diadematus dragline silk fibroin, and the amphiphilic sequence (AEAEAKAK)2. Although the (AEAEAKAK) sequence is not a silk-derived sequence, it has been shown to form very stable /8-sheet stmctures in aqueous solution (111). Proteins... 

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