1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.

@article{Okon19921HNA,
  title={1H NMR assignments and secondary structure of human beta 2-microglobulin in solution.},
  author={M S Okon and Patrick Bray and Dragica Vuceli{\'c}},
  journal={Biochemistry},
  year={1992},
  volume={31 37},
  pages={8906-15}
}
Sequence-specific resonance assignments of human beta 2-microglobulin (M(r) 12,000) and its secondary structure are determined by 2D NMR techniques. The protein is found to contain two antiparallel beta-sheets each of four beta-strands with the beta-sheets being connected by a single disulfide linkage. No evidence for any regular helical structure is found. Amide proton-solvent-exchange rate constants and 3JHN alpha coupling constants are evaluated.