• Bifunctional Avidin with Covalently Modifiable Ligand Binding Site 

      Leppiniemi, Jenni; Määttä, Juha A E; Hammaren, Henrik; Soikkeli, Mikko; Laitaoja, Mikko; Jänis, Janne; Kulomaa, Markku S; Hytönen, Vesa P (2011)
      The extensive use of avidin and streptavidin in life sciences originates from the extraordinary tight biotin-binding affinity of these tetrameric proteins. Numerous studies have been performed to modify the biotin-binding ...
    • Modification of the loops in the ligand-binding site turns avidin into a steroid-binding protein 

      Riihimäki, Tiina A; Hiltunen, Soili; Rangl, Martina; Nordlund, Henri R; Määttä, Juha A E; Ebner, Andreas; Hinterdorfer, Peter; Kulomaa, Markku S; Takkinen, Kristiina; Hytönen, Vesa P (2011)
      Background Engineered proteins, with non-immunoglobulin scaffolds, have become an important alternative to antibodies in many biotechnical and therapeutic applications. When compared to antibodies, tailored proteins may ...
    • Structural and functional characteristics of xenavidin, the first frog avidin from Xenopus tropicalis 

      Määttä, Juha A E; Helppolainen, Satu H; Hytönen, Vesa P; Johnson, Mark S; Kulomaa, Markku S; Airenne, Tomi T; Nordlund, Henri R (2009)
      Background Avidins are proteins with extraordinarily high ligand-binding affinity, a property which is used in a wide array of life science applications. Even though useful for biotechnology and nanotechnology, the ...
    • Structure of bradavidin - C-terminal residues act as intrinsic ligands 

      Leppiniemi, Jenni; Grönroos, Toni; Määttä, Juha A E; Johnson, Mark S; Kulomaa, Markku S; Hytönen, Vesa P; Airenne, Tomi T (2012)
      Abstract Top Bradavidin is a homotetrameric biotin-binding protein from Bradyrhizobium japonicum, a nitrogen fixing and root nodule-forming symbiotic bacterium of the soybean. Wild-type (wt) bradavidin has 138 amino ...