Abstract
Data have been measured at two temperatures, 293 K and 107 K, for a crystal of a thyrotropin-releasing hormone analogue, pGlu-Phe-D-Pro-psi [CN4]-NMe, C20H25N7O3, and the structures solved and refined. The tripeptide contains a tetrazole ring which mimics a cis-peptide bond at the C terminus. An intermolecular hydrogen bond exists between two molecules related by the twofold screw axis, resulting in infinite chains of hydrogen-bonded peptide molecules. Because of the folding and packing of the molecules, there are no intermolecular contacts of less than 4 A to the N atom of the phenylalanine residue.
| Original language | English |
|---|---|
| Pages (from-to) | 2575-2579 |
| Number of pages | 5 |
| Journal | Acta crystallographica. Section C, Crystal structure communications |
| Volume | 51 ( Pt 12) |
| DOIs | |
| State | Published - Dec 15 1995 |
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