Talk:Autochaperone

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Another definition of an autochaperone is broader. It can be considered an intra molecular chaperone, it is  part of a protein that assists in assembly. This can be seen with the C-terminus of  some  tailspikes of the bacteriophages. A good example is the Bacillus phage ø29 tailspike crystalized in Michael Rossman's lab.

Xiang, Y., Leiman, P.G., Li, L., Grimes, S., Anderson, D.L., and Rossmann, M.G. (2009). Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol Cell 34, 375-386.

and the E Coli K phages tailspike Stummeyer, K., Dickmanns, A., Muhlenhoff, M., Gerardy-Schahn, R., and Ficner, R. (2005). Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. Nat Struct Mol Biol 12, 90-96.

Schulz, E.C., Dickmanns, A., Urlaub, H., Schmitt, A., Muhlenhoff, M., Stummeyer, K., Schwarzer, D., Gerardy-Schahn, R., and Ficner, R. (2010). Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nat Struct Mol Biol 17, 210-215.

20:03, 9 November 2010 (UTC)18.79.0.59 (talk)Cameron Haase-Pettingell MIT Biology chulz, E.C., Dickmanns, A., Urlaub, H., Schmitt, A., Muhlenhoff, M., Stummeyer, K., Schwarzer, D., Gerardy-Schahn, R., and Ficner, R. (2010). Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding. Nat Struct Mol Biol 17, 210-215.

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