An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S
- 25 February 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (11), 3444-3446
- https://doi.org/10.1021/ja0397254
Abstract
A new reverse turn, replacing one of the native type II‘ β-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.Keywords
This publication has 28 references indexed in Scilit:
- β-Barrel membrane protein folding and structure viewed through the lens of α-hemolysinBiochimica et Biophysica Acta (BBA) - Biomembranes, 2002
- Arsenic Mobility and Groundwater Extraction in BangladeshScience, 2002
- Probing the Structural Determinants of Type II‘ β-Turn Formation in Peptides and ProteinsJournal of the American Chemical Society, 2002
- En route to supramolecular functional plasticity: artificial β-barrels, the barrel-stave motif, and related approachesChemical Society Reviews, 2001
- Foldamers: A ManifestoAccounts of Chemical Research, 1998
- Isothermal Compressibility and Pressure Dependence of the Crystal Structures of the Superconducting Charge-Transfer Salt κ-(BEDT-TTF)2Cu(NCS)2 [BEDT-TTF = Bis(ethylenedithio)tetrathiafulvalene]Acta crystallographica Section B, Structural science, crystal engineering and materials, 1997
- Molecular Simulations of β-Sheet TwistingJournal of Molecular Biology, 1996
- Artificial β-sheetsChemical Society Reviews, 1996
- Thermoluminescence dating of sediment baked by Iava flows of the Chaîne des PuysNature, 1978
- Conformational analysis of the sugar ring in nucleosides and nucleotides. New description using the concept of pseudorotationJournal of the American Chemical Society, 1972