International Tables for Crystallography (2006). Vol. F. ch. 23.2, pp. 579-587   | 1 | 2 |
https://doi.org/10.1107/97809553602060000715

Chapter 23.2. Protein–ligand interactions

Contents

  • 23.2. Protein–ligand interactions  (pp. 579-587) | html | pdf | chapter contents |
    A. E. Hodel and F. A. Quiocho
    • 23.2.1. Introduction  (p. 579) | html | pdf |
    • 23.2.2. Protein–carbohydrate interactions  (pp. 579-580) | html | pdf |
      • 23.2.2.1. Carbohydrate recognition at the atomic level  (pp. 579-580) | html | pdf |
    • 23.2.3. Metals  (pp. 580-581) | html | pdf |
      • 23.2.3.1. Metals important in protein function and structure  (pp. 580-581) | html | pdf |
    • 23.2.4. Protein–nucleic acid interactions  (pp. 581-585) | html | pdf |
      • 23.2.4.1. The DNA double helix  (pp. 581-583) | html | pdf |
      • 23.2.4.2. Single-stranded sequence-nonspecific DNA–protein interactions  (p. 583) | html | pdf |
      • 23.2.4.3. RNA  (p. 583) | html | pdf |
      • 23.2.4.4. Transfer RNA  (pp. 583-584) | html | pdf |
      • 23.2.4.5. Stem loops  (p. 584) | html | pdf |
      • 23.2.4.6. Single-stranded sequence-nonspecific RNA–protein interactions  (p. 584) | html | pdf |
      • 23.2.4.7. The recognition of alkylated bases  (pp. 584-585) | html | pdf |
    • 23.2.5. Phosphate and sulfate  (pp. 585-587) | html | pdf |
      • 23.2.5.1. Dominant role of local dipoles in stabilization of isolated charges  (p. 586) | html | pdf |
      • 23.2.5.2. Short hydrogen bonds  (p. 586) | html | pdf |
      • 23.2.5.3. Non-complementary negative electrostatic surface potential of protein sites specific for anions  (pp. 586-587) | html | pdf |
    • References | html | pdf |
    • Figures
      • Fig. 23.2.2.1. The atomic recognition of carbohydrates by a protein  (p. 579) | html | pdf |
      • Fig. 23.2.4.1. A schematic diagram of the base pairs of DNA showing the hydrogen-bonding groups which may be used in the sequence-specific recognition of DNA  (p. 581) | html | pdf |
      • Fig. 23.2.4.2. (a) A space-filling model of B-DNA showing the relative accessibility of the major and minor grooves  (p. 582) | html | pdf |
      • Fig. 23.2.4.3. A comparison of the orientations of α-helices bound in the major groove  (p. 582) | html | pdf |
      • Fig. 23.2.4.4. The sequence-nonspecific recognition of single-stranded nucleic acid  (p. 583) | html | pdf |
      • Fig. 23.2.4.5. The specific recognition of the messenger RNA 7-methylguanosine cap  (p. 584) | html | pdf |
      • Fig. 23.2.5.1. 12 hydrogen-bonding interactions between the phosphate-binding protein (PBP) and phosphate  (p. 585) | html | pdf |
      • Fig. 23.2.5.2. Seven hydrogen-bonding interactions between the sulfate-binding protein (SBP) and sulfate  (p. 586) | html | pdf |
      • Fig. 23.2.5.3. Electrostatic surface potential of (a) the phosphate-binding protein and (b) flavodoxin  (p. 587) | html | pdf |
    • Tables
      • Table 23.2.3.1. Metal ions associated with proteins  (p. 580) | html | pdf |