[ meld een fout in dit record ]mandje (0): toevoegen | toon Print deze pagina
The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation
Claverie, P.; Vigano, C.; Ruysschaert, J.-M.; Gerday, C.; Feller, G. (2003). The precursor of a psychrophilic α-amylase: structural characterization and insights into cold adaptation. Biochimica et Biophysica Acta-Proteins and Proteomics 1649(2): 119-122. https://dx.doi.org/10.1016/S1570-9639(03)00184-5
In: Biochimica et Biophysica Acta-Proteins and Proteomics. ELSEVIER SCIENCE BV: Amsterdam. ISSN 1570-9639; e-ISSN 0006-3002, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoord
    Marien/Kust
Author keywords
    alpha-amylase; psychrophile; autotransporter; microcalorimetry; infraredspectroscopy
Auteurs  Top 
  • Claverie, P.
  • Vigano, C.
  • Ruysschaert, J.-M.
Abstract
    The α-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted β-barrel of autotransporters, this C-terminal propeptide displays a noticeable α-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.
Alle informatie in het Integrated Marine Information System (IMIS) valt onder het VLIZ Privacy beleid Top | Auteurs 
IMIS is ontwikkeld en wordt gehost door het VLIZ.