International Tables for Crystallography
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International Tables for Crystallography (2006). Vol. F, Section 22.2.7.1 |
Hydrogen bonding in biological macromolecules International Tables for Crystallography (2012). Vol. F, ch. 22.3, pp. 721-729 [ doi:10.1107/97809553602060000887 ] Abstract 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 multi-volume series 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.