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 ψ, ω and φ 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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Document Type: Review Article
Affiliations: School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW.
Publication date: 2002-04-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.