1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.

@article{Hanzawa19901HNM,
  title={1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.},
  author={Hiroyuki Hanzawa and Ichio Shimada and Takashi Kuzuhara and Hiroto Komano and Daisuke Kohda and Fuyuhiko Inagaki and Shunji Natori and Yoji Arata},
  journal={FEBS letters},
  year={1990},
  volume={269 2},
  pages={413-20}
}
The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in… CONTINUE READING

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