Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 35–38

Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms

  • Helena Tossavainen
  • Satu H. Helppolainen
  • Juha A. E. Määttä
  • Tero Pihlajamaa
  • Vesa P. Hytönen
  • Markku S. Kulomaa
  • Perttu Permi
Article

Abstract

Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin’s ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin’s feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AVR4). In this chimeric protein a 23-residue segment in avidin has been replaced with the corresponding sequence found in AVR4, and a point mutation at subunit interface 1–3 (and 2–4) has been introduced. Here we report the backbone and sidechain resonance assignments of the biotin-bound form of ChiAVD(I117Y) as well as the backbone resonance assignments of the free form.

Keywords

Biotin Chimeric avidin NMR Thermostability Ligand binding 

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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Helena Tossavainen
    • 1
  • Satu H. Helppolainen
    • 1
    • 2
  • Juha A. E. Määttä
    • 2
    • 3
  • Tero Pihlajamaa
    • 1
  • Vesa P. Hytönen
    • 2
    • 3
  • Markku S. Kulomaa
    • 2
    • 3
  • Perttu Permi
    • 1
  1. 1.Program in Structural Biology and BiophysicsInstitute of BiotechnologyHelsinkiFinland
  2. 2.Institute of Biomedical TechnologyUniversity of Tampere, Tampere University HospitalTampereFinland
  3. 3.BioMediTechTampereFinland

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