Hydrophobic dipeptides: the final piece in the puzzle | Zendy

Görbitz Carl Henrik | Zendy

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Hydrophobic dipeptides: the final piece in the puzzle

Author(s) -

Görbitz Carl Henrik

Publication year - 2018

Publication title -

acta crystallographica section b

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.604

H-Index - 33

ISSN - 2052-5206

DOI - 10.1107/s2052520618007151

Subject(s) - dipeptide , leucine , valine , phenylalanine , isoleucine , hydrogen bond , amino acid , chemistry , crystal structure , tripeptide , alanine , peptide , stereochemistry , crystallography , organic chemistry , molecule , biochemistry

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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