Thermal unfolding in a GCN4-like leucine zipper: 13C alpha NMR chemical shifts and local unfolding curves.

@article{Holtzer1997ThermalUI,
  title={Thermal unfolding in a GCN4-like leucine zipper: 13C alpha NMR chemical shifts and local unfolding curves.},
  author={Marilyn Emerson Holtzer and E G Lovett and Dana Andr{\'e} d'Avignon and Alfred Holtzer},
  journal={Biophysical journal},
  year={1997},
  volume={73 2},
  pages={1031-41}
}
13C alpha chemical shifts and site-specific unfolding curves are reported for 12 sites on a 33-residue, GCN4-like leucine zipper peptide (GCN4-lzK), ranging over most of the chain and sampling most heptad positions. Data were derived from NMR spectra of nine synthetic, isosequential peptides bearing 99% 13C alpha at sites selected to avoid spectral overlap in each peptide. At each site, separate resonances appear for unfolded and folded forms, and most sites show resonances for two folded forms… CONTINUE READING

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