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• W2031141888 abstract "Heteronuclear NMR methods have been used to elucidate the secondary structure and the general tertiary fold of the protein NodF from Rhizobium leguminosarum. A similarity to acyl carrier proteins of the fatty acid synthase system had been suggested by the presence of a phosphopantetheine prosthetic group and a short stretch of sequence homology near the prosthetic group attachment site. NMR results suggest that the structural homology extends well beyond this region. Both proteins have three well-formed helices which fold in a parallel-antiparallel fashion and a prosthetic group attachment site near the beginning of the second helix." @default.
• W2031141888 created "2016-06-24" @default.
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• W2031141888 date "1996-06-10" @default.
• W2031141888 modified "2023-09-30" @default.
• W2031141888 title "NMR investigations of the structural properties of the nodulation protein, NodF, from<i>Rhizobium leguminosarum</i>and its homology with<i>Escherichia coli</i>acyl carrier protein" @default.
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• W2031141888 doi "https://doi.org/10.1016/0014-5793(96)00512-1" @default.
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