NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.

@article{Kobayashi1999NMRAO,
  title={NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.},
  author={Norihiro Kobayashi and Stefan Freund and Jean Chatellier and Ralph Zahn and A. R. Fersht},
  journal={Journal of molecular biology},
  year={1999},
  volume={292 1},
  pages={181-90}
}
A detailed structural analysis of interactions between denatured proteins and GroEL is essential for an understanding of its mechanism. Minichaperones constitute an excellent paradigm for obtaining high-resolution structural information about the binding site and conformation of substrates bound to GroEL, and are particularly suitable for NMR studies. Here, we used transferred nuclear Overhauser effects to study the interaction in solution between minichaperone GroEL(193-335) and a synthetic… CONTINUE READING