NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.

@article{Alexandrescu2000NMREF,
  title={NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN.},
  author={Andrei T. Alexandrescu and François Lamour and Victor A Jaravine},
  journal={Journal of molecular biology},
  year={2000},
  volume={295 2},
  pages={239-55}
}
The acid-denatured form of the protein LysN aggregates reversibly at pH 2.0. The strength of self-association increases with increasing Cl(-) anion concentration. At low concentrations of protein or Cl(-) anion, resonances of denatured LysN are in slow exchange with a minor form of the protein, which shows native-like NMR chemical shifts. The minor native-like resonances increase in intensity with increasing protein concentration, demonstrating that a native-like monomer fold is stabilized on… CONTINUE READING