An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core.

@article{Park1997AnEI,
  title={An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core.},
  author={Si Hong Park and Karyn T O'Neil and Heinrich Roder},
  journal={Biochemistry},
  year={1997},
  volume={36 47},
  pages={14277-83}
}
The folding kinetics of a 57-residue IgG binding domain of streptococcal protein G has been studied under varying solvent conditions, using stopped-flow fluorescence methods. Although GB1 has been cited as an example of a protein that obeys a two-state folding mechanism, the following kinetic observations suggest the presence of an early folding intermediate. Under stabilizing conditions (low denaturant concentrations, especially in the presence of sodium sulfate), the kinetics of folding shows… CONTINUE READING

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