Oriented immobilization of farnesylated proteins by the thiol-ene reaction.

@article{Weinrich2010OrientedIO,
  title={Oriented immobilization of farnesylated proteins by the thiol-ene reaction.},
  author={Dirk Weinrich and Po-Chiao Lin and P. Jonkheijm and Uyen T. T. Nguyen and H. Schr{\"o}der and C. Niemeyer and K. Alexandrov and R. Goody and H. Waldmann},
  journal={Angewandte Chemie},
  year={2010},
  volume={49 7},
  pages={
          1252-7
        }
}
Anchoring the protein: Proteins were immobilized rapidly under mild conditions by thiol-ene photocoupling between S-farnesyl groups attached to a genetically encodable “CAAX-box” tetrapeptide sequence (A is aliphatic) at the C terminus of the protein and surface-exposed thiols (see scheme). This method enables the oriented covalent immobilization of proteins directly from expression lysates without additional purification or derivatization steps. 
Direct immobilization of oxyamine-modified proteins from cell lysates.
Supramolecularly oriented immobilization of proteins using cucurbit[8]uril.
Reversible and oriented immobilization of ferrocene-modified proteins.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 44 REFERENCES
Regio- and chemoselective covalent immobilization of proteins through unnatural amino acids.
Photochemical surface patterning by the thiol-ene reaction.
Site-selective protein immobilization by Staudinger ligation.
Therapeutic intervention based on protein prenylation and associated modifications
Zinc-catalyzed sulfur alkyation:insights from protein farnesyltransferase.
...
1
2
3
4
5
...