Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonance.

@article{Lian1992DeterminationOT,
  title={Determination of the solution structures of domains II and III of protein G from Streptococcus by 1H nuclear magnetic resonance.},
  author={Lu Yun Lian and Jeremy P Derrick and Michael J. Sutcliffe and Joy C. Yang and Gordon C. K. Roberts},
  journal={Journal of molecular biology},
  year={1992},
  volume={228 4},
  pages={1219-34}
}
We have used 1H nuclear magnetic resonance spectroscopy to determine the solution structures of two small (61 and 64 residue) immunoglobulin G (IgG)-binding domains from protein G, a cell-surface protein from Streptococcus strain G148. The two domains differ in sequence by four amino acid substitutions, and differ in their affinity for some subclasses of IgG. The structure of domain II was determined using a total of 478 distance restraints, 31 phi and 9 chi 1 dihedral angle restraints; that of… CONTINUE READING

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