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Water and Biological Macromolecules pp 63–97Cite as

Hydration of Amino Acids in Protein Crystals

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Part of the book series: Topics in Molecular and Structural Biology ((TMSB))

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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Authors
  1. Julia M. Goodfellow
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  2. Narmada Thanki
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  3. Janet M. Thornton
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Editor information

Editors and Affiliations

  1. Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Strasbourg, France

    Eric Westhof

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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

  • Online ISBN: 978-1-349-12359-9

  • eBook Packages: EngineeringEngineering (R0)

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