Structure and conformation of linear peptides
- 1 November 1984
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 24 (5) , 437-441
- https://doi.org/10.1111/j.1399-3011.1984.tb03142.x
Abstract
The tripeptide, glycyl‐glycyl‐L‐valine, crystallizes as a dihydrate in the monoclinic space group P21, with a = 5.786(1), b = 7.954(2), c = 14.420(3)A, β= 93.85(2)d̀, Z = 2. The structure was solved by direct methods and refined to an R‐value of 0.040 for 876 observed reflections. The molecule exists as a zwitterion in the crystal. The peptide planes show significant deviations from planarity. The chain conformation resembles a reverse turn if the orientation of the carboxyl group is also taken into account. An intramolecular water bridge links the amino and carboxyl ends of the molecule. The crystal packing involves spatial segregation of polar and nonpolar moieties.Keywords
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