By means of conformational analysis, the spatial structure and conformational potential of the H-Tyr-Ala-Gly-Ala-Val-Val-Asn-Asp-Leu-OH molecule, which corresponds to sequence 329-337 of the subunit 2 C-terminal region of the herpes virus ribonucleotide reductase, were studied. It was shown that its spatial organization can be described by a set of 17 low-energy conformations of the backbone. The "reverse conformational problem" for this molecule was solved to enable the prediction of a series of synthetic analogues matching the set of low-energy, potentially physiologically active conformations.
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