Automated analysis of NMR assignments and structures for proteins

Curr Opin Struct Biol. 1999 Oct;9(5):635-42. doi: 10.1016/s0959-440x(99)00019-6.


Recent developments in protein NMR technology have provided spectral data that are highly amenable to analysis by advanced computer software systems. Specific data collection strategies, coupled with these computer programs, allow automated analysis of extensive backbone and sidechain resonance assignments and three-dimensional structures for proteins of 50 to 200 amino acids.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Automation / methods
  • Fibroblast Growth Factor 2 / chemistry
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation*
  • Protein Structure, Secondary
  • Proteins / chemistry*


  • Proteins
  • Fibroblast Growth Factor 2