International Tables for Crystallography (2006). Vol. F, ch. 22.2, pp. 546-552   | 1 | 2 |
doi: 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 |
      • 22.2.3.1. Proteins  (p. 546) | html | pdf |
      • 22.2.3.2. Nucleic acids  (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 |
        • 22.2.5.3.1. Helices  (p. 548) | html | pdf |
        • 22.2.5.3.2. β-sheets  (pp. 548-549) | html | pdf |
        • 22.2.5.3.3. Turns  (p. 549) | html | pdf |
        • 22.2.5.3.4. Aspects of in-plane geometry  (p. 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 |
      • 22.2.6.1. DNA  (p. 551) | html | pdf |
      • 22.2.6.2. RNA  (p. 551) | html | pdf |
    • 22.2.7. Non-conventional hydrogen bonds  (pp. 551-552) | html | pdf |
      • 22.2.7.1. C—H···O hydrogen bonds  (pp. 551-552) | html | pdf |
      • 22.2.7.2. Hydrogen bonds involving sulfur atoms  (p. 552) | html | pdf |
      • 22.2.7.3. Amino-aromatic hydrogen bonding  (p. 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 |