Detalle de: An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S
| Title | An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S |
| Abstract |
A new reverse turn, replacing one of the native type II' beta-turns in the cyclic peptide antibiotic gramicidin S, induced by a furanoid sugar amino acid is revealed. The C3-hydroxyl function plays a pivotal role by acting as a H-bond acceptor, consequently flipping the amide bond between residues i and i + 1, as was established by NMR and X-ray crystallographic analysis. |
| Apa Reference | Grotenbreg, G. M., Timmer, M. S. M., Llamas-Saiz, A. L., Verdoes, M., van der Marel, G. A., van Raaij, M. J., Overkleeft, H. S., & Overhand, M. (2004). An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S. Journal of the American Chemical Society, 126(11), 3444–3446. 10.1021/ja0397254 |
| Doi | 10.1021/ja0397254 |
| Publication Date | 25 Feb 2004 |
| Publication Type | Article |
| Researcher | Mark van Raaij |
| Ontology | Experimental structure determination |
| Research Groups | Structural Biology of Virus Proteins |
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