Site-selective protein immobilization by Staudinger ligation.

@article{Watzke2006SiteselectivePI,
  title={Site-selective protein immobilization by Staudinger ligation.},
  author={Anja Watzke and Maja K{\"o}hn and Marta Guti{\'e}rrez-Rodr{\'i}guez and Ron Wacker and Hendrik V Schr{\"o}der and Rolf Breinbauer and Jürgen Kuhlmann and Kirill Alexandrov and Christof M. Niemeyer and Roger S. Goody and Herbert Waldmann},
  journal={Angewandte Chemie},
  year={2006},
  volume={45 9},
  pages={
          1408-12
        }
}
A sticky situation: A site-specific immobilization of proteins onto a glass surface may allow the creation of protein microarrays. This approach relies on the Staudinger ligation between azide-modified proteins and a phosphane-functionalized glass surface. 
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References

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Site-specific protein immobilization by Staudinger ligation.
The Staudinger ligation between an azido-protein and a phosphinothioester-derivatized surface is demonstrated to be an effective means for the site-specific, covalent immobilization of a protein.
Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication.
TLDR
This new method was used to immobilize two fluorescent proteins and a functional SH3 domain using a protein microarrayer and is based in the chemoselective reaction between a protein C-terminal alpha-thioester and a modified surface containing N-Terminal Cys residues.
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TLDR
The current state of knowledge on the Staudinger ligation and its application both for the preparation of bioconjugates and as a ligation method in chemical biology are described.
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TLDR
It is shown that proteins containing azidohomoalanine can be selectively modified in the presence of other cellular proteins by means of Staudinger ligation with triarylphosphine reagents and incorporation of azide-functionalized amino acids into proteins in vivo provides opportunities for protein modification under native conditions and selective labeling of proteins in the intracellular environment.
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TLDR
The results indicate that the novel dendrimer‐activated surfaces display a surface coverage with capture oligomers about twofold greater than that with conventional microarrays containing linear chemical linkers.
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We report here the use of an intein-mediated protein ligation strategy for the synthesis of glycoproteins and proteins containing various molecular probes. Several simple cysteine derivatives are
Probing glycosyltransferase activities with the Staudinger ligation.
TLDR
A novel glycosyltransferase assay that exploits their unnatural substrate tolerance and the unique chemical reactivity of the azide is described, applicable to any glycosoltransferase or group-transfer enzyme that tolerates unnatural azido substrates.
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TLDR
Miniaturized assays that accommodate extremely low sample volumes and enable the rapid, simultaneous processing of thousands of proteins are developed to facilitate subsequent studies of protein function.
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