TY - JOUR
T1 - A thyrotropin-releasing hormone analogue
T2 - pGlu-Phe-D-Pro-psi [CN4]-NMe at 293 and 107 K.
AU - Howell, P. L.
AU - Pangborn, W. A.
AU - Marshall, G. R.
AU - Zabrocki, J.
AU - Smith, G. D.
PY - 1995/12/15
Y1 - 1995/12/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=16144366838&partnerID=8YFLogxK
U2 - 10.1107/s0108270194014952
DO - 10.1107/s0108270194014952
M3 - Article
C2 - 8588858
AN - SCOPUS:16144366838
SN - 0108-2701
VL - 51 ( Pt 12)
SP - 2575
EP - 2579
JO - Acta crystallographica. Section C, Crystal structure communications
JF - Acta crystallographica. Section C, Crystal structure communications
ER -