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• W2081138607 abstract "The solution three-dimensional structure of the protonated [Leu7]-surfactin, an hepta-peptide extracted from Bacillus subtilis, has been determined from two-dimensional 1Hnmr performed in 2H6-dimethylsulfoxide and combined with molecular modeling. Experimental data included 9 coupling constants, 61 nuclear Overhauser effect derived distances, NH temperature coefficients, and 13C relaxation times. Two distance geometry (DISMAN) protocols converged toward models of the structure and the best of them were refined by restrained and unrestrained molecular dynamics (GROMOS). Two structures in accord with the set of experimental constraints are presented. Both are characterized by a “horse saddle” topology for ring atoms on which are attached the two polar Glu and Asp side chains showing an orientation clearly opposite to that of the C11–13 aliphatic chain. Amphipathic and surface properties of surfactin are certainly related to the existence of such minor polar and a major hydrophobic domains. The particular “claw” configuration of acidic residues observed in surfactin gives important clues for the understanding of its cation binding and transporting ability. © 1994 John Wiley & Sons, Inc." @default.
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• W2081138607 date "1994-07-01" @default.
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• W2081138607 title "Solution three-dimensional structure of surfactin: A cyclic lipopeptide studied by¹H-nmr, distance geometry, and molecular dynamics" @default.
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• W2081138607 doi "https://doi.org/10.1002/bip.360340716" @default.
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