International Tables for Crystallography (2006). Vol. F. ch. 22.2, pp. 546-552
https://doi.org/10.1107/97809553602060000711 |
Chapter 22.2. Hydrogen bonding in biological macromolecules
Contents
- 22.2. Hydrogen bonding in biological macromolecules (pp. 546-552) | html | pdf | chapter contents |
- 22.2.1. Introduction (p. 546) | html | pdf |
- 22.2.2. Nature of the hydrogen bond (p. 546) | html | pdf |
- 22.2.3. Hydrogen-bonding groups (pp. 546-547) | html | pdf |
- 22.2.4. Identification of hydrogen bonds: geometrical considerations (p. 547) | html | pdf |
- 22.2.5. Hydrogen bonding in proteins (pp. 547-551) | html | pdf |
- 22.2.5.1. Contribution to protein folding and stability (pp. 547-548) | html | pdf |
- 22.2.5.2. Saturation of hydrogen-bond potential (p. 548) | html | pdf |
- 22.2.5.3. Secondary structures (pp. 548-549) | html | pdf |
- 22.2.5.4. Side-chain hydrogen bonding (pp. 549-550) | html | pdf |
- 22.2.5.5. Hydrogen bonds with water molecules (pp. 550-551) | html | pdf |
- 22.2.6. Hydrogen bonding in nucleic acids (p. 551) | html | pdf |
- 22.2.7. Non-conventional hydrogen bonds (pp. 551-552) | html | pdf |
- References | html | pdf |
- Figures
- Fig. 22.2.2.1. Hydrogen-bonding configurations (p. 546) | html | pdf |
- Fig. 22.2.3.1. Hydrogen-bonding potential of protein functional groups (p. 547) | html | pdf |
- Fig. 22.2.3.2. Hydrogen-bonding potential of nucleic acid bases guanine (G), adenine (A), cytosine (C) and thymine (T) in their normal canonical forms. (p. 547) | html | pdf |
- Fig. 22.2.4.1. Suggested criteria for identifying likely hydrogen bonds (p. 547) | html | pdf |
- Fig. 22.2.5.1. Distribution of side-chain–main-chain hydrogen bonds as a function of the separation (Δ a.a.) along the polypeptide between the side-chain (sch) and main-chain (mch) groups involved (p. 549) | html | pdf |
- Fig. 22.2.5.2. Schematic representations of common classes of side-chain–main-chain hydrogen bonds (a) in turns and (b) at helix N-termini (p. 549) | html | pdf |
- Fig. 22.2.5.3. Typical scatter plots showing the distribution of hydrogen-bonding partners around protein side chains, shown for (a) Asn or Gln and (b) Tyr (p. 550) | html | pdf |
- Fig. 22.2.6.1. Hydrogen-bonding interactions in RNA tertiary structure (p. 551) | html | pdf |