Water molecules hydrogen bonding to aromatic acceptors of amino acids: the structure of Tyr-Tyr-Phe dihydrate and a crystallographic database study on peptides.
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.
Steiner
T
T
Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany. steiner@chemie.fu-berlin.de
Schreurs
A M
AM
Kanters
J A
JA
Kroon
J
J
D000596:Amino Acids / Q000737:chemistry*; D003461:Crystallography; D018360:Crystallography, X-Ray; D016208:Databases, Factual; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D000596:Amino Acids; D009842:Oligopeptides; D010455:Peptides; D014867:Water; C067117:tyrosyl-tyrosyl-phenylalanine