Acta Crystallographica, Section C: Crystal Structure Communications 2010-11-01

L-histidyl-L-serine 3.7-hydrate: water channels in the crystal structure of a polar dipeptide.

Carl Henrik Görbitz

Index: Acta Crystallogr. C 66 , o531-534, (2010)

Full Text: HTML

Abstract

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.


Related Compounds

Related Articles:

Ternary nickel(II) complexes as hydrolytic DNA-cleavage agents.

2006-02-01

[Chem. Biodivers. 3 , 231-244, (2006)]

Ternary zinc(II)-dipeptide complexes for the hydrolytic cleavage of DNA at physiological pH.

2005-05-01

[Chem. Biodivers. 2 , 672-683, (2005)]

Novel peptide-based copper(II) complexes for total hydrolytic cleavage of DNA.

2005-10-01

[Chem. Biodivers. 2 , 1338-1350, (2005)]

Copper(II) complexes containing N,N-donor ligands and dipeptides act as hydrolytic DNA-cleavage agents.

2004-06-01

[Chem. Biodivers. 1 , 839-853, (2004)]

More Articles...