International Tables for Crystallography

Hydrogen bonding in biological macromolecules
E. N. Baker. International Tables for Crystallography (2006). Vol. F, ch. 22.2, pp. 546-552  [ doi:10.1107/97809553602060000711 ]


Hydrogen bonds are weak non-covalent interactions, but their directional nature and the large number of hydrogen-bonding groups mean that they play a critical role in the structure and function of proteins and nucleic acids. Analyses of three-dimensional structures, particularly of proteins, reveal many consistent patterns, which are described in this review. Protein structures show almost complete saturation of hydrogen-bonding potential. Helices, β-strands, β-turns and γ-turns all show characteristic C=O···HN geometries, with helices having a variety of termination patterns. Local interactions are very common for main-chain···side-chain hydrogen bonds and may help direct protein folding. Non-local interactions, although fewer in number, can be very important for structural stability, and bound water molecules, because of their double-donor, double-acceptor capability, can play critical roles in satisfying overall hydrogen-bonding requirements. Finally, there is also a growing realization that non-conventional hydrogen bonds may play a more important role than hitherto recognized.

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About International Tables for Crystallography

International Tables for Crystallography is the definitive resource and reference work for crystallography. The series consists of eight volumes and comprises articles and tables of data relevant to crystallographic research and to applications of crystallographic methods in all sciences concerned with the structure and properties of materials.