X-ray crystallographic signature of supramolecular triple helix formation from a water soluble synthetic tetrapeptide.
Single crystal X-ray diffraction studies on the water soluble, synthetic tetrapeptide Tyr(1)-Aib(2)-Tyr(3)-Val(4) with a non-coded amino acid residue (Aib: [small alpha]-amino isobutyric acid) reveal that the peptide adopts an "S"-shaped molecular structure which self-assembles to form a supramolecular triple helix using various non-covalent interactions including water mediated hydrogen bonds in the solid state.
Das
Apurba Kumar
AK
Department of Physics, Indian Institute of Science, Bangalore-560012, India.
Haldar
Debasish
D
Hegde
Raghurama P
RP
Shamala
N
N
Banerjee
Arindam
A
D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D012995:Solubility; D014867:Water / Q000737:chemistry*
D010455:Peptides; D014867:Water