Molecular structure heterogeneity of gramicidin analogs incorporated into SDS micelles: a NMR study
by Hinton, James F.; Jordan, John Bradley; Horne, E.
The effects of glycine, alanine and valine substitution for leucine upon the species heterogeneity of gramicidin A incorporated into SDS micelles have been investigated. The sequential replacement of the leucine residues at positions 10, 12 and 14 produced multiple beta-helical forms of the gramicidin A analogs as shown by H-1 NMR spectroscopy. These results reveal the complexity of the interaction of amino acid residue side chain with the SDS micelle environment in controlling the formation of a single channel species or multiple helical forms. Clearly, a potential problem may arise if one assumes that the solubilization of the peptide, gramicidin, in micelles indicates the existence of a single form of the peptide. (C) 2002 Elsevier Science B.V. All rights reserved.
- Journal of Molecular Structure
- Start Page
- 1872-8014; 0022-2860