Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme

  title={Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme},
  author={Denis Canet and Alexander M. Last and Paula Tito and Margaret Sunde and Andrew Spencer and David B. Archer and Christina Redfield and Carol V Robinson and Christopher M. Dobson},
  journal={Nature Structural Biology},
Hydrogen exchange experiments monitored by NMR and mass spectrometry reveal that the amyloidogenic D67H mutation in human lysozyme significantly reduces the stability of the β-domain and the adjacent C-helix in the native structure. In addition, mass spectrometric data reveal that transient unfolding of these regions occurs with a high degree of cooperativity. This behavior results in the occasional population of a partially structured intermediate in which the three α-helices that form the… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.
65 Citations
34 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 65 extracted citations


Publications referenced by this paper.
Showing 1-10 of 34 references

Hydrogen exchange of proteins in partially folded states : a quadrupole time - of - flight approach . Methods Enzymol . In the press (

  • P. Tito, C. V. Robinson
  • 2002

Designing conditions for in vitro formation of amyloid protofilaments and fibrils

  • F. Chiti
  • Proc . Natl . Acad . Sci . USA
  • 1999

Similar Papers

Loading similar papers…