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. 1998 Jan 1;54(Pt 1):25-31.
doi: 10.1107/s0907444997007981.

Water molecules hydrogen bonding to aromatic acceptors of amino acids: the structure of Tyr-Tyr-Phe dihydrate and a crystallographic database study on peptides

T Steiner  1 , A M Schreurs, J A Kanters, J Kroon
Affiliations

Water molecules hydrogen bonding to aromatic acceptors of amino acids: the structure of Tyr-Tyr-Phe dihydrate and a crystallographic database study on peptides

T Steiner et al. Acta Crystallogr D Biol Crystallogr. .

Abstract

The crystal structure of Tyr-Tyr-Phe dihydrate contains a hydrogen bond formed between a water molecule and the Phe side chain. The geometry is centered with a distance of 3.26 A between the water O atom and the aromatic centroid. In a database study on hydrated peptides, four related examples are found which exhibit a wide variability of hydrogen-bond geometries. The intermolecular surroundings of the water molecules are inspected, showing that they are typically involved in complex networks of conventional and non-conventional hydrogen bonds. Possible relevance for protein hydration is given.

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