First observation of a beta-turn conformation fused with the oxy-analogue of an alpha-turn: the molecular structure of a model peptide of the C-terminal part of gramicidin A |
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| Authors: | E Benedetti A Bavoso B Di Blasio V Pavone C Pedone C Toniolo G M Bonora |
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| Affiliation: | 1. The Cecil H. and Ida Green Center for Reproductive Biology Sciences The University of Texas Southwestern Medical School Dallas, Texas, USA;2. the Department of Biochemistry The University of Texas Southwestern Medical School Dallas, Texas, USA;3. the Department of Obstetrics-Gynecology The University of Texas Southwestern Medical School Dallas, Texas, USA |
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| Abstract: | The molecular structure of N-tert-butyloxycarbonyl-D-leucyl-L-phenylalanyl ethanolamide (t-Boc-D-Leu-L-Phe-EA), a protected analogue of the C-terminal dipeptide of the membrane-active linear antibiotic gramicidin A, has been determined by X-ray diffraction. One of the two independent molecules in the asymmetric unit is characterized by a chain reversal stabilized by an intramolecular, three-centre, double hydrogen bonding. It represents the first experimental evidence for a beta-turn conformation fused with the oxy-analogue of an alpha-turn. |
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| Keywords: | To whom correspondence should be addressed. |
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