Conserved folding pathways of alpha-lactalbumin and lysozyme revealed by kinetic CD, fluorescence, NMR, and interrupted refolding experiments.

@article{Schlepckow2008ConservedFP,
  title={Conserved folding pathways of alpha-lactalbumin and lysozyme revealed by kinetic CD, fluorescence, NMR, and interrupted refolding experiments.},
  author={Kai Schlepckow and Julia Wirmer and Annett Bachmann and Thomas Kiefhaber and Harald Schwalbe},
  journal={Journal of molecular biology},
  year={2008},
  volume={378 3},
  pages={686-98}
}
In this report, it is shown by a combination of stopped-flow CD, fluorescence, and time-resolved NMR studies that the Ca(2+)-induced refolding of bovine alpha-lactalbumin (BLA) at constant denaturant concentration (4 M urea) exhibits triple-exponential kinetics. In order to distinguish between parallel folding pathways and a strictly sequential formation of the native state, interrupted refolding experiments were conducted. We show here that the Ca(2+)-induced refolding of BLA involves parallel… CONTINUE READING