Abstract
The crystal structure of L-valyl-L-leucine acetonitrile solvate presented here adds to 24 previously reported structures of dipeptides constructed from the five nonpolar amino acids L-alanine, L-valine, L-isoleucine, L-leucine and L-phenylalanine. It thus constitutes the final piece in the 5 × 5 puzzle of hydrophobic dipeptide structures. This opportunity is taken to review the crystal packing arrangements and hydrogen-bonding preferences of a rather unique group of substances, with updated information on the various hydrogen-bonding patterns and the associated peptide conformations.
Publisher
International Union of Crystallography (IUCr)
Subject
Materials Chemistry,Metals and Alloys,Atomic and Molecular Physics, and Optics,Electronic, Optical and Magnetic Materials
Cited by
17 articles.
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