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- W2088049114 abstract "An acyclic tripeptide based on a heterochiral d-pro-l-pro template shows a propensity to exist as a 310 helical conformation and can be cyclized, via ring-closing metathesis, to the corresponding cyclic tetrapeptides without disrupting the helical conformations in CDCl3 as well as in DMSO-d6 solutions. The detailed conformational studies were carried out by using NMR spectroscopy, X-ray crystallography, molecular dynamic simulations, and circular dichroism spectroscopy." @default.
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- W2088049114 date "2004-02-26" @default.
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- W2088049114 title "Synthesis and Conformational Studies of Novel Cyclic Peptides Constrained into a 3<sub>10</sub> Helical Structure by a Heterochiral <scp>d</scp>-Pro-<scp>l</scp>-Pro Dipeptide Template" @default.
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- W2088049114 doi "https://doi.org/10.1021/jo030282w" @default.
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