Talk:Autochaperone

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Comments[edit]

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 Cite error: A <ref> tag is missing the closing </ref> (see the help page).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.</ref> ^[1]

References

^ iang, 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.

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[1] , 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.

[1]