Chapter 19.7 Nuclear magnetic resonance (NMR) spectroscopy

Crystallography of biological macromolecules

First Online Edition (2006)

Part 19. Other experimental techniques

  1. K. Wüthrich

Published Online: 1 JAN 2006

DOI: 10.1107/97809553602060000704

International Tables for Crystallography

International Tables for Crystallography

How to Cite

Wüthrich, K. 2006. Nuclear magnetic resonance (NMR) spectroscopy. International Tables for Crystallography. F:19:19.7:464–479.

Author Information

  1. Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule‐Hönggerberg, CH‐8093 Zürich, Switzerland

Publication History

  1. Published Online: 1 JAN 2006



A brief description is presented of the standard protocol for NMR structure determination of proteins and nucleic acids in solution. The main focus is then on comparisons of corresponding information that can be obtained by X‐ray crystallography and by solution NMR spectroscopy. In particular, these comparisons cover information on internal mobility of protein molecules and data obtained on solvation of biological macromolecules. Considering the complementarity of the information obtained from the two methods, ways are indicated in which X‐ray diffraction in single crystals and NMR spectroscopy in solution can be combined to obtain more comprehensive information on the behaviour of biological macromolecules.


  • conformational equilibria;
  • dynamic processes;
  • nuclear magnetic resonance;
  • ring flipping;
  • solvation;
  • structure determination