Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor.

@article{Wagner1984AmideprotonES,
  title={Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor.},
  author={Gerhard Wagner and Chariklia I. Stassinopoulou and Kurt W{\"u}thrich},
  journal={European journal of biochemistry},
  year={1984},
  volume={145 2},
  pages={431-6}
}
The backbone amide proton exchange with the solvent was investigated in 2H2O solutions of the basic pancreatic trypsin inhibitor and two chemical modifications thereof, which were obtained by transamination of the N-terminus and by cleavage of the disulfide bond 14-38, respectively. The three proteins have nearly identical conformations, but the stability with respect to thermal denaturation is markedly different. Exchange rates for a large number of individually assigned amide protons located… CONTINUE READING