L-histidyl-L-serine 3.7-hydrate: water channels in the crystal structure of a polar dipeptide.
Dipeptides may form nanotubular structures with pore diameters in the range 3.2-10 Å. These compounds normally contain at least one and usually two hydrophobic residues, but L-His-L-Ser hydrate, C(9)H(14)N(4)O(4)·3.7H(2)O, with two hydrophilic residues, forms large polar channels filled with ordered as well as disordered water molecules.
Department of Chemistry, University of Oslo, Oslo, Norway. c.h.gorbitz@kjemi.uio.no
Carl Henrik
CH
Görbitz
D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D014867:Water / Q000737:chemistry
D004151:Dipeptides; C516949:histidylserine; D014867:Water