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

Chapter index

Bidentate hydrogen bonding 23.2.2.1
Calcium-binding proteins 23.2.3.1
calmodulin 23.2.3.1
staphylococcal nuclease 23.2.3.1
Calmodulin 23.2.3.1
Carbohydrate-binding proteins 23.2.2
Cooperative hydrogen bonding 23.2.2.1, 23.2.4.1
DNA
interactions with proteins 23.2.4.1, 23.2.4.2
Enzyme catalysis
role of metal ions 23.2.3
Hard metals 23.2.3.1
Hydrogen bonding
bidentate 23.2.2.1
cooperative 23.2.2.1, 23.2.4.1
short, in phosphate-binding protein 23.2.5.2
Myoglobin 23.2.3
Nucleic acids
interactions with proteins 23.2.4
Phosphate-binding protein 23.2.5
short hydrogen bond to phosphate 23.2.5.2
Polarizability
hard and soft metals 23.2.3.1
Protein–carbohydrate recognition 23.2.2, 23.2.2.1
Protein function
role of metal ions 23.2.3, 23.2.3.1
Protein–ligand interactions 23.2.1
carbohydrates 23.2.2, 23.2.2.1
metals 23.2.3, 23.2.3.1
phosphate 23.2.5
sulfate 23.2.5
Protein–nucleic acid interactions 23.2.4
DNA 23.2.4.1, 23.2.4.2
RNA 23.2.4.3, 23.2.4.6
transfer RNA 23.2.4.4
Protein stability
role of metal ions 23.2.3
RNA
interactions with proteins 23.2.4.3, 23.2.4.6
Secondary structure
of RNA 23.2.4.3
Soft metals 23.2.3.1, 23.2.3.1
Staphylococcal nuclease 23.2.3.1
Sulfate-binding protein 23.2.5
Tertiary structure
of RNA 23.2.4.3
Transfer RNA
interactions with proteins 23.2.4.4