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Hydrophobic dipeptides: the final piece in the puzzle

Görbitz, Carl Henrik
Journal article; PublishedVersion; Peer reviewed
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169.+Val-Leu.puzzle.pdf (1.534Mb)
Year
2018
Permanent link
http://urn.nb.no/URN:NBN:no-75735

CRIStin
1599955

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  • Kjemisk institutt [843]
  • CRIStin høstingsarkiv [15898]
Original version
Acta Crystallographica. Section B: Structural Science, Crystal Engineering and Materials. 2018, 74, 311-318, DOI: https://doi.org/10.1107/S2052520618007151
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.
 
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