Biomolecular NMR Assignments

, Volume 4, Issue 2, pp 151–154

Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

  • Tony Collins
  • Manolis Matzapetakis
  • Helena Santos
Article

DOI: 10.1007/s12104-010-9230-0

Cite this article as:
Collins, T., Matzapetakis, M. & Santos, H. Biomol NMR Assign (2010) 4: 151. doi:10.1007/s12104-010-9230-0

Abstract

Enzymes produced by psychrophilic organisms have successfully overcome the low temperature challenge and evolved to maintain high catalytic rates in their permanently cold environments. As an initial step in our attempt to elucidate the cold-adaptation strategies used by these enzymes we report here the 1H, 15N and 13C assignments for the reduced form of a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

Keywords

Cold-adapted enzymesDsbAReduced oxidoreductasePseudoalteromonas haloplanktis TAC125

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Tony Collins
    • 1
  • Manolis Matzapetakis
    • 1
  • Helena Santos
    • 1
  1. 1.Instituto de Tecnologia Química e BiológicaUniversidade Nova de LisboaOeirasPortugal