Kringle 4 from human plasminogen:1H-nuclear magnetic resonance study of the interactions between ω-amino acid ligands and aromatic residues at the lysine-binding site

@article{Llins2007Kringle4F,
  title={Kringle 4 from human plasminogen:1H-nuclear magnetic resonance study of the interactions between ω-amino acid ligands and aromatic residues at the lysine-binding site},
  author={Miguel Llin{\'a}s and Annelisa Motta and Ario de Marco and Richard A. Laursen},
  journal={Journal of Biosciences},
  year={2007},
  volume={8},
  pages={121-139}
}
The interactions of theω-amino acid ligandsε-aminocaproic acid andp-benzylaminesulphonic acid with the isolated kringle 4 domain from human plasminogen have been investigated by1H-nuclear magnetic resonance spectroscopy at 300 and 600 MHz. Overall, the data indicate that binding either ligand does not cause the kringle to undergo significant conformational… CONTINUE READING