Comparison of the NMR and X-Ray Structures of Hirudin

  • G. Marius Clore
  • Angela M. Gronenborn
Chapter
Part of the NATO ASI Series book series (NSSA, volume 225)

Abstract

The solution structure of hirudin determined by NMR is compared to that of the subsequently determined crystal structure. The well-defined region common to both structures is the core of the N-terminal domain which comprises residues 2–30 and 37–48. The backbone conformation of the two structures is very similar with an atomic rms difference of <1 Å. A number of side chains have essentially identical conformations in the NMR and crystal structures. The majority of side chains, however, are highly surface exposed and disordered both in solution and in the crystal.

Keywords

Disulfide Bridge Backbone Atom Backbone Carbonyl Determine Crystal Structure Identical Conformation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • G. Marius Clore
    • 1
  • Angela M. Gronenborn
    • 1
  1. 1.National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of HealthLaboratory of Chemical PhysicsBethesdaUSA

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