Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation.

@article{Weik2002EvidenceFT,
  title={Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation.},
  author={Martin Weik and Jacqueline Berg{\`e}s and Maria L Raves and Piet Gros and Se{\'a}n McSweeney and Israel Silman and Joel L. Sussman and Chantal Hou{\'e}e-L{\'e}vin and Raimond B G Ravelli},
  journal={Journal of synchrotron radiation},
  year={2002},
  volume={9 Pt 6},
  pages={342-6}
}
Irradiation of proteins with intense X-ray radiation produced by third-generation synchrotron sources generates specific structural and chemical alterations, including breakage of disulfide bonds and decarboxylation. In this paper, disulfide bond lengths in irradiated crystals of the enzyme Torpedo californica acetylcholinesterase are examined based on quantum simulations and on experimental data published previously. The experimental data suggest that one disulfide bond elongates by… CONTINUE READING