Young Investigator Award Lecture. Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR

Protein Sci. 1994 Mar;3(3):372-90. doi: 10.1002/pro.5560030302.


The recent development of a whole panoply of multidimensional heteronuclear-edited and -filtered NMR experiments has revolutionized the field of protein structure determination by NMR, making it possible to extend the methodology from the 10-kDa limit of conventional 2-dimensional NMR to systems up to potentially 35-40 kDa. The basic strategy for solving 3-dimensional structures of larger proteins and protein-ligand complexes in solution using 3- and 4-dimensional NMR spectroscopy is summarized, and the power of these methods is illustrated using 3 examples: interleukin-1 beta, the complex of calmodulin with a target peptide, and the specific complex of the transcription factor GATA-1 with its cognate DNA target site.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calmodulin / chemistry
  • DNA / chemistry
  • DNA-Binding Proteins / chemistry*
  • Erythroid-Specific DNA-Binding Factors
  • GATA1 Transcription Factor
  • Humans
  • Ligands
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Molecular Structure
  • Protein Conformation
  • Proteins / chemistry*
  • Sequence Homology, Amino Acid
  • Transcription Factors / chemistry


  • Calmodulin
  • DNA-Binding Proteins
  • Erythroid-Specific DNA-Binding Factors
  • GATA1 Transcription Factor
  • GATA1 protein, human
  • Ligands
  • Proteins
  • Transcription Factors
  • DNA