Historical Perspective

Development of NMR: Structural Biology Since the Early 1990s

  1. Dennis A. Torchia

Published Online: 15 JUN 2012

DOI: 10.1002/9780470034590.emrhp1081



How to Cite

Torchia, D. A. 2012. Development of NMR: Structural Biology Since the Early 1990s. eMagRes. .

Author Information

  1. National Institutes of Health, Bethesda, MD, USA

Publication History

  1. Published Online: 15 JUN 2012


This article traces advances of NMR applications in structural biology that have taken place in the past 20 years. It begins with a brief summary of pioneering work in the field that is covered more fully in the first volume of this encyclopedia(see Becker, Edwin D.: Development of NMR: From the Early Beginnings to the Early 1990s). This introduction is followed by three main sections. The first two trace developments of the past two decades that have dramatically increased the quantity, quality, and complexity of biomolecular structures solved by NMR in solution and solid states. These sections cover advances in multidimensional, double and triple resonance solution- and solid-state NMR methodology that, together with various schemes for isotopic enrichment, provide sequential signal assignments as well as structural restraints, enabling structures of great biological significance to be solved. Developments in data processing and structure computation that have played a major role in the success of structure determination are noted, as are methods for guiding structure prediction with limited sets of NMR restraints. A few biomolecular structures solved by NMR methods are presented at the end of each section, in order to show the wide variety of structure-function relationships revealed by contemporary NMR techniques. In the final section, the development of methods for investigating the dynamics of biomolecules in solution and solid states is traced. Topics covered are measurements of spin relaxation rates, residual anisotropic interactions, and chemical exchange, as well as the use of these measurements to extract information about biomolecular dynamics on the timescale ranging from picoseconds to many seconds. The section concludes with examples illustrating how information about biomolecular dynamics has aided in understanding function.


  • NMR;
  • biomolecule;
  • structure;
  • restraints;
  • NOE;
  • chemical shift;
  • RDC;
  • paramagnetic;
  • MAS;
  • recoupling;
  • dynamics;
  • spin relaxation;
  • order parameter;
  • exchange;