Tobias Schnitzer, Joseph F. Woods, Nils Trapp, Helma Wennemers
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引用次数: 0
Abstract
Oligoprolines adopt the well-defined polyproline II (PPII) helical conformation, even at a short chain length of six residues. These rigid peptides are versatile molecular rulers and scaffolds, yet there has been great difficulty in obtaining single crystals for X-ray crystal structure analysis to probe their conformation in the solid state. Here, we report a crystal structure of an oligoproline hexamer bearing an N-terminal terephthalic acid moiety. Comparison with that of a previously obtained crystal structure of a closely related hexaproline revealed influence of the terminal functional groups and the solvent on the crystal packing.
期刊介绍:
Helvetica Chimica Acta, founded by the Swiss Chemical Society in 1917, is a monthly multidisciplinary journal dedicated to the dissemination of knowledge in all disciplines of chemistry (organic, inorganic, physical, technical, theoretical and analytical chemistry) as well as research at the interface with other sciences, where molecular aspects are key to the findings. Helvetica Chimica Acta is committed to the publication of original, high quality papers at the frontier of scientific research. All contributions will be peer reviewed with the highest possible standards and published within 3 months of receipt, with no restriction on the length of the papers and in full color.