Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy

Crit Rev Biochem Mol Biol. 1995;30(5):351-85. doi: 10.3109/10409239509083489.


With the advent of multidimensional heteronuclear-edited and -filtered NMR experiments, the field of three-dimensional structure determination by NMR has again increased in scope, making it possible to move the technology beyond the approximately 10 kDa limit inherent to conventional two-dimensional NMR to systems up to potentially 35 to 40 kDa. This article outlines the basic strategies for solving three-dimensional structures of larger systems, in particular, protein complexes and multimeric proteins using three- and four-dimensional NMR spectroscopy, summarizes the key experiments, and illustrates the power of these methods using several examples of protein-DNA, protein-peptide complexes, and oligomeric proteins from the authors' laboratories.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • DNA-Binding Proteins / chemistry
  • Humans
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Proteins / chemistry*
  • Sequence Alignment


  • DNA-Binding Proteins
  • Proteins