Abstract
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.
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