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 determinati on by NMR has again increased in scope, making it possible to move the technology beyond the approximately 10 kDa limit inherent to conventi onal two-dimensional NMR to systems upto potentially 35 to 40 kDa. Thi s article outlines the basic strategies for solving three-dimensional structures of larger systems, in particular, protein complexes and mul timeric proteins using three- and four-dimensional NMR spectroscopy, s ummarizes the key experiments, and illustrates the power of these meth ods using several examples of protein-DNA, protein-peptide complexes, and oligomeric proteins from the authors' laboratories.