Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.

@article{Drohat1996SolutionSO,
  title={Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.},
  author={Alexander C. Drohat and J C Amburgey and Frits Abildgaard and Mary R. Starich and Donna M. Baldisseri and David J. Weber},
  journal={Biochemistry},
  year={1996},
  volume={35 36},
  pages={11577-88}
}
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta subunit (91 residues) has four alpha-helices and a small antiparallel beta-sheet, consistent with two predicted helix-loop-helix Ca(2+)-binding domains known as EF-hands [Amburgey et al. (1995) J. Biomol. NMR 6, 171-179]. The three-dimensional solution structure of apo-S100B(beta beta) from rat has been determined using 2672 distance (14.7… CONTINUE READING

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