Abstract
The interactions of water molecules with proteins have been of interest for a long time. This stems from the role of water in protein folding, during which apolar side-chains tend to be buried in the centre of the protein (thus reducing their contact with aqueous solvent). On folding, intramolecular hydrogen bonds are formed at the expense of protein—solvent hydrogen bonds. The fully folded protein retains many interactions with its aqueous media, since not all polar main chain or side-chain groups are involved in intramolecular hydrogen bonds, leaving unfilled potential hydrogen bond donor and acceptor atoms. Many apolar groups are also found on the surface in contact with water molecules.
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Goodfellow, J.M., Thanki, N., Thornton, J.M. (1993). Hydration of Amino Acids in Protein Crystals. In: Westhof, E. (eds) Water and Biological Macromolecules. Topics in Molecular and Structural Biology. Palgrave, London. https://doi.org/10.1007/978-1-349-12359-9_3
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DOI: https://doi.org/10.1007/978-1-349-12359-9_3
Publisher Name: Palgrave, London
Print ISBN: 978-1-349-12361-2
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