An Integrated Mass Spectrometry Based Approach to Probe the Structure of the Full-Length Wild-Type Tetrameric p53 Tumor Suppressor.

@article{Arlt2017AnIM,
  title={An Integrated Mass Spectrometry Based Approach to Probe the Structure of the Full-Length Wild-Type Tetrameric p53 Tumor Suppressor.},
  author={Christian Arlt and Vanessa Judith Flegler and Christian Ihling and Mathias Sch{\"a}fer and Iris Thondorf and Andrea Sinz},
  journal={Angewandte Chemie},
  year={2017},
  volume={56 1},
  pages={
          275-279
        }
}
We present an integrated approach for investigating the topology of proteins through native mass spectrometry (MS) and cross-linking/MS, which we applied to the full-length wild-type p53 tetramer. For the first time, the two techniques were combined in one workflow to obtain not only structural insight in the p53 tetramer, but also information on the cross-linking efficiency and the impact of cross-linker modification on the conformation of an intrinsically disordered protein (IDP). P53 cross… 

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