Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins.

@article{Zimmermann1995SolutionSO,
  title={Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins.},
  author={Grant R. Zimmermann and Pascale Legault and Michael E Selsted and Arthur Pardi},
  journal={Biochemistry},
  year={1995},
  volume={34 41},
  pages={13663-71}
}
The solution structure is reported for bovine neutrophil beta-defensin-12 (BNBD-12), a member of the beta-defensin family of antimicrobial peptides. Structural constraints in the form of proton-proton distances, dihedral angles, and hydrogen bond constraints were derived from two-dimensional, homonuclear magnetic resonance spectroscopy experiments. The three-dimensional structure of BNBD-12 was calculated using distance geometry and restrained molecular dynamics. An ensemble of structures with… CONTINUE READING

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