Chapter 19.7 Nuclear magnetic resonance (NMR) spectroscopy
Crystallography of biological macromolecules
Second Online Edition (2012)
Part 19. Other experimental techniques
Published Online: 14 APR 2012
© International Union of Crystallography 2006
International Tables for Crystallography
How to Cite
Wüthrich, K. 2012. Nuclear magnetic resonance (NMR) spectroscopy. International Tables for Crystallography. F:19:19.7:615–619.
- Published Online: 14 APR 2012
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;
- structure determination