Presence of distinct virtual backbone torsion angles in dipeptide conformers.
Zwitterionic dipeptides have recently been shown to exist in water mainly as nine conformational forms with specific combinations of backbone Psi, omega and Phi torsions, which allows conformer-specific molecular recognition of peptide ligands by proteins. Here, we show that pairs of virtual backbone torsions can also define these nine conformational forms, and that comparing these virtual torsions in dipeptides with those of backbone-modified pseudopeptides offers an improved procedure for evaluating peptidomimetics for therapeutic applications.
School of Biological Sciences, University of Wales Bangor, Gwynedd LL57 2UW, UK.
S
S
Gupta
B M
BM
Grail
J W
JW
Payne
D002151:Calorimetry; D007477:Ions; D008024:Ligands; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D021381:Protein Transport
D007477:Ions; D008024:Ligands; D010455:Peptides