Structures of protein complexes by multidimensional heteronuclear magnetic resonance spectroscopy.
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.
Gronenborn
A M
AM
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Clore
G M
GM
D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D004268:DNA-Binding Proteins; D011506:Proteins