Marsh, Richard E. ; Narasimha Murthy, M. R. ; Venkatesan, K. (1977) Peptide conformations. Crystal structures of tert-butyloxycarbonylglycyl-L-proline and its benzyl ester Journal of the American Chemical Society, 99 (4). pp. 1251-1256. ISSN 0002-7863
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Official URL: http://pubs.acs.org/doi/abs/10.1021/ja00446a042
Related URL: http://dx.doi.org/10.1021/ja00446a042
Abstract
The crystal structures of tert-butyloxycarbonylglycyl-L-proline and its benzyl ester are respond. Both molecules show similar, extended conformation and there is no hint of the folded conformation that had earlier been suggested for tert-butyloxycarbonylglycyl-L-proline. It us shows that differences in the IR spectra of the two crystals, which had been interpreted in terms of an intramolecular hydrogen bond in the orthombic space group P212121, with cill dimensions a=5.743 (2), b=23.849 (5), and c=10.440 (2) Å for the free peptide and a=15.381 (3), b=19.112 (4), c=6.638 (2) Å for the benzyl ester. Least-squares refinement led to R indxes of 0.049 and 0.037 for 1344 and 2273 reflections with positive net intensity.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to American Chemical Society. |
| ID Code: | 66677 |
| Deposited On: | 27 Oct 2011 04:02 |
| Last Modified: | 27 Oct 2011 04:02 |
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