High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine.

@article{Ito2011HighresolutionXA,
  title={High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine.},
  author={Leonardo Yu Ito and Kentaro Shiraki and Takanori Matsuura and Masaki Okumura and Kazuya Hasegawa and Seigo Baba and Hiroshi Yamaguchi and Takashi Kumasaka},
  journal={Protein engineering, design & selection : PEDS},
  year={2011},
  volume={24 3},
  pages={
          269-74
        }
}
While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg-lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions… CONTINUE READING

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