Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR

@article{Cave2000BackboneDO,
  title={Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR},
  author={J. Cave and D. Wemmer and W. Kremer},
  journal={Protein Science},
  year={2000},
  volume={9}
}
Backbone dynamics of the basic/helix‐loop‐helix domain of Pho4 from Saccharomyces cerevisae have been probed by NMR techniques, in the absence of DNA, nonspecifically bound to DNA and bound to cognate DNA. Alpha proton chemical shift indices and nuclear Overhauser effect patterns were used to elucidate the secondary structure in these states. These secondary structures are compared to the co‐crystal complex of Pho4 bound to a cognate DNA sequence (Shimizu T, Toumoto A, Ihara K, Shimizu M… Expand
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