• 1 January 1981
    • journal article
    • research article
    • Vol. 18  (2) , 195-202
Abstract
The model tripeptide tBuCO-L-Pro-Me-D-Ala-NHMe [tBu = tert-butyloxycarbonyl] crystallizes in both anhydrous (1) and monohydrated (2) states: 1, monoclinic space group C2 with a = 20.030 (2) .ANG., b = 5.836 (2) .ANG., c = 14.958 (3) .ANG. and .beta. = 94.11 (1); 2, orthorhombic space group P212121 with a = 6.971 (6) .ANG., b = 11.766 (3) .ANG. and c = 22.394 (8) .ANG.. Both crystal structures were solved by X-ray diffraction to characterize the influence of water on the molecular structure. The anhydrous molecule accommodates the well-known, .beta.II-folded conformation with 3 trans amide functions and an intramolecular i + 3 .fwdarw. i H-bond. In the hydrated molecule, water is inserted in a loop containing 12 atoms and induces some conformational changes of the peptide backbone.

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