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Conformational properties of Pro–Pro sequences. I. Crystal structures of two dipeptides with L-Pro-L-Pro and L-Pro-D-Pro sequences

✍ Scribed by André Aubry; Bernard Vitoux; Michel Marraud

Publisher
Wiley (John Wiley & Sons)
Year
1985
Tongue
English
Weight
487 KB
Volume
24
Category
Article
ISSN
0006-3525

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✦ Synopsis

The crystal structures of Bu'CO-L-Pro-L-Pro-NHMe, H 2 0 ( I : monoclinic; P2,; a = 6.662, b = 11.067, c = 12.205 A; P = 96.28") and Bu'CO-L-Pro-DPro-NHMe (2: monoclinic; P2,; a = 10.770, b = 15.039, c = 11.325 .&; p = 110.00") have been solved by x-ray diffraction. Structure 1 accommodates an open disposition with intermolecular interactions involving the water molecule, while 2 is PII-folded by an intramolecular i + 3 i hydrogen bond. In both derivatives, small thermal parameters are indicative of fairly fixed conformations for the proline rings. Comparison between conformations of either isolated or adjacent L-Pro residues in the crystal structures of unstrained oligopeptides shows that the conformational properties of L-Pro-L-Pro sequences are probably a simple combination of those found for isolated L-Pro residues.

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