Immobilization of biotinylated hGBP1 in a defined orientation on surfaces is crucial for uniform interaction with analyte proteins and catalytic activity.

@article{Syguda2012ImmobilizationOB,
  title={Immobilization of biotinylated hGBP1 in a defined orientation on surfaces is crucial for uniform interaction with analyte proteins and catalytic activity.},
  author={Adrian Syguda and Andreas Kerstan and Tatjana Ladnorg and Florian St{\"u}ben and Christof W{\"o}ll and Christian Herrmann},
  journal={Langmuir : the ACS journal of surfaces and colloids},
  year={2012},
  volume={28 15},
  pages={6411-8}
}
Guanylate binding proteins (GBPs) belong to the dynamin superfamily of large GTP binding proteins. A biochemical feature common to these proteins is guanosine-triphosphate (GTP) binding leading to self-assembly of the proteins, and this in turn results in higher catalytic GTP hydrolysis activity. In the case of human guanylate binding protein 1 (hGBP1… CONTINUE READING