Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.

@article{Folkers1989SolutionSO,
  title={Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.},
  author={P. Folkers and G. Clore and P. Driscoll and J. Dodt and S. K{\"o}hler and A. Gronenborn},
  journal={Biochemistry},
  year={1989},
  volume={28 6},
  pages={
          2601-17
        }
}
  • P. Folkers, G. Clore, +3 authors A. Gronenborn
  • Published 1989
  • Chemistry, Medicine
  • Biochemistry
  • The solution structure of recombinant wild-type hirudin and of the putative active site mutant Lys-47----Glu has been investigated by nuclear magnetic resonance (NMR) spectroscopy at 600 MHz. The 1H NMR spectra of the two hirudin variants are assigned in a sequential manner with a combination of two-dimensional NMR techniques. Some assignments made in our previous paper [Sukumaran, D. K., Clore, G. M., Preuss, A., Zarbock, J., & Gronenborn, A. M. (1987) Biochemistry 26, 333-338] were found to… CONTINUE READING

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