Secondary structure of barley serine proteinase inhibitor 2 determined by proton nuclear magnetic resonance spectroscopy

@article{Kjr1987SecondarySO,
  title={Secondary structure of barley serine proteinase inhibitor 2 determined by proton nuclear magnetic resonance spectroscopy},
  author={Mogens Kj{\ae}r and Flemming M. Poulsen},
  journal={Carlsberg Research Communications},
  year={1987},
  volume={52},
  pages={355-362}
}
The secondary structure of BSPI-2 has been determined using information obtained exclusively from1H-NMR recordings of Nuclear Overhauser effects, coupling constants and hydrogen exchange rates. It is shown that the protein contains one α-helix and a six-stranded β-sheet. Four of the strands form an anti-parallel β-sheet, and two form a parallel. In addition, six turns and one half turn have been identified. The segment containing the active site shows no secondary structure. This secondary… CONTINUE READING

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