Urea unfolding of peptide helices as a model for interpreting protein unfolding.

@article{Scholtz1995UreaUO,
  title={Urea unfolding of peptide helices as a model for interpreting protein unfolding.},
  author={J. Martin Scholtz and Doug Barrick and Eunice J. York and James Mcd Stewart and Robert L. Baldwin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 1},
  pages={185-9}
}
To provide a model system for understanding how the unfolding of protein alpha-helices by urea contributes to protein denaturation, urea unfolding was measured for a homologous series of helical peptides with the repeating sequence Ala-Glu-Ala-Ala-Lys-Ala and chain lengths varying from 14 to 50 residues. The dependence of the helix propagation parameter of the Zimm-Bragg model for helix-coil transition theory (s) on urea molarity ([urea]) was determined at 0 degree C with data for the entire… CONTINUE READING

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