Conformations and interactions of histone H2A (F2A2, ALK).

@article{Bradbury1975ConformationsAI,
  title={Conformations and interactions of histone H2A (F2A2, ALK).},
  author={E. Bradbury and P. Cary and C. Crane-Robinson and H. Rattle and M. Boublik and P. Sautière},
  journal={Biochemistry},
  year={1975},
  volume={14 9},
  pages={
          1876-85
        }
}
Conformational changes in histone H2A (ALK, F2A2, IIbl) as a function of ionic strength and pH have been followed using high resolution nuclear magnetic resonance (NMR), circular dichroism (CD), and infrared (ir). While change in pH from 3 to 7 (no added salt) causes little structural change, added salt induces the formation of both alpha helix (28 percent maximum) and intermolecular associates in the region of the molecule between 25 and 113. No beta structure was observed at high salt. By the… Expand
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