International Tables for Crystallography (2012). Vol. F. ch. 19.7, pp. 615-619   | 1 | 2 |
https://doi.org/10.1107/97809553602060000873

Chapter 19.7. Nuclear magnetic resonance (NMR) spectroscopy

Contents

  • 19.7. Nuclear magnetic resonance (NMR) spectroscopy  (pp. 615-619) | html | pdf | chapter contents |
    K. Wüthrich
    • 19.7.1. Complementary roles of NMR in solution and X-ray crystallography in structural biology  (p. 615) | html | pdf |
    • 19.7.2. A standard protocol for NMR structure determination of proteins and nucleic acids  (pp. 615-617) | html | pdf |
    • 19.7.3. Combined use of single-crystal X-ray diffraction and solution NMR for structure determination  (p. 617) | html | pdf |
    • 19.7.4. NMR studies of solvation in solution  (pp. 617-618) | html | pdf |
    • 19.7.5. NMR studies of rate processes and conformational equilibria in three-dimensional macromolecular structures  (p. 618) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 19.7.2.1. Diagram outlining the course of a macromolecular structure determination by NMR in solution  (p. 615) | html | pdf |
      • Fig. 19.7.2.2. (a) Sequential resonance assignment based on sequential 1H–1H NOEs  (p. 616) | html | pdf |
      • Fig. 19.7.2.3. Polypeptide backbone of 19 energy-refined conformers selected to represent the NMR solution structure of the Antennapedia homeodomain  (p. 617) | html | pdf |
      • Fig. 19.7.5.1. 180° ring flips of tyrosine and phenylalanine about the Cβ—C1 bond  (p. 618) | html | pdf |