Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation.

@article{Costenaro2002LinkBP,
  title={Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation.},
  author={Lionel Costenaro and Giuseppe Zaccai and Christine Maria Isabel Ebel},
  journal={Biochemistry},
  year={2002},
  volume={41 44},
  pages={13245-52}
}
Malate dehydrogenase (Hm MalDH) from the extreme halophile Haloarcula marismortui is a very acidic protein with extensive ion binding properties. It is a good model for the study of solvation-solubility relationships. We measured the small-angle neutron or X-ray scattering profiles of folded and stable Hm MalDH at various protein concentrations and derived the second virial coefficients A(2). In NaCl, CsCl, KF, KCl, and NaCH(3)CO(2), A(2) values are positive, indicating globally repulsive… CONTINUE READING