The monohydrates of the four polar dipeptides L-seryl-L-asparagine, L-seryl-L-tyrosine, L-tryptophanyl-L-serine and L-tyrosyl-L-tryptophan.
The crystal structures of the four dipeptides L-seryl-L-asparagine monohydrate, C(7)H(13)N(3)O(5) x H(2)O, L-seryl-L-tyrosine monohydrate, C(12)H(16)N(2)O(5) x H(2)O, L-tryptophanyl-L-serine monohydrate, C(14)H(17)N(3)O(4) x H(2)O, and L-tyrosyl-L-tryptophan monohydrate, C(20)H(21)N(3)O(4) x H(2)O, are dominated by extensive hydrogen-bonding networks that include cocrystallized solvent water molecules. Side-chain conformations are discussed on the basis of previous observations in dipeptides. These four dipeptide structures greatly expand our knowledge on dipeptides incorporating polar residues such as serine, asparagine, threonine, tyrosine and tryptophan.
Görbitz
Carl Henrik
CH
Department of Chemistry, University of Oslo, PO Box 1033 Blindern, N-0315 Oslo, Norway. c.h.gorbitz@kjemi.uio.no
Hartviksen
Lars Male
LM
D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D014867:Water / Q000737:chemistry*
D004151:Dipeptides; D014867:Water