WATER-MOLECULES HYDROGEN-BONDING TO AROMATIC ACCEPTORS OF AMINO-ACIDS- THE STRUCTURE OF TYR-TYR-PHE DIHYDRATE AND A CRYSTALLOGRAPHIC DATABASE STUDY ON PEPTIDES

Authors
STEINER T SCHREURS AMM KANTERS JA KROON J
Citation
T. Steiner et al., WATER-MOLECULES HYDROGEN-BONDING TO AROMATIC ACCEPTORS OF AMINO-ACIDS- THE STRUCTURE OF TYR-TYR-PHE DIHYDRATE AND A CRYSTALLOGRAPHIC DATABASE STUDY ON PEPTIDES, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 25-31
Citations number
34
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
1
Pages
25 - 31
Database
ISI
SICI code
0907-4449(1998)54:<25:WHTAAO>2.0.ZU;2-X
Abstract
The crystal structure of Tyr-Tyr-Phe dihydrate contains a hydrogen bon d formed between a water molecule and the Phe side chain. The geometry is centered with a distance of 3.26 Angstrom 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 hy drogen-bond geometries. The intermolecular surroundings of the water m olecules are inspected, showing that they are typically involved in co mplex networks of conventional and non-conventional hydrogen bonds. Po ssible relevance for protein hydration is given.