Hydrogen exchange experiments monitored by NMR and mass spectrometry reveal that the amyloidogenic D67H mutation in human lysozyme significantly reduces the stability of the beta-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 alpha-helices that for...Expand abstract
- Publication status:
- Publisher copy:
- Copyright date:
Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
If you are the owner of this record, you can report an update to it here: Report update to this record