Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry

@article{Veenstra1998ZincinducedCC,
  title={Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry},
  author={Timothy D. Veenstra and K. L. Johnson and Andy J. Tomlinson and T. A. Craig and Raj Kumar and Stephen Naylor},
  journal={Journal of the American Society for Mass Spectrometry},
  year={1998},
  volume={9},
  pages={8-14}
}
Electrospray ionization mass Spectrometry (ESI-MS) was used to measure conformational changes within the DNA-binding domain of the vitamin D receptor (VDR DBD) upon binding zinc (Zn2+). As increasing concentrations of Zn2+ were added to the VDR DBD, a gradual shift in the mass envelope to lower charge states was observed in the multiply charged spectrum. The shift in the charge states was correlated to changes observed in the far-ultraviolet circular dichroic (far-UV CD) spectrum of the protein… Expand
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