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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation.

The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted beta-barrel of autotransporters, this C-terminal propeptide displays a noticeable alpha-helix content. It is connected to the enzyme by a disordered linker and has no significant interaction with the catalytic domain. The microcalorimetric pattern of the precursor also demonstrates that the stability of protein domains may evolve differently.[1]

References

  1. The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation. Claverie, P., Vigano, C., Ruysschaert, J.M., Gerday, C., Feller, G. Biochim. Biophys. Acta (2003) [Pubmed]
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