Abstract
We report the backbone chemical shift assignments of the acyl-acyl carrier protein (ACP) intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum. The acyl-ACP intermediates butyryl (C(4)), -octanoyl (C(8)), -decanoyl (C(10)), -dodecanoyl (C(12)) and -tetradecanoyl (C(14))-ACPs display marked changes in backbone HN, C(alpha) and C(beta) chemical shifts as a result of acyl chain insertion into the hydrophobic core. Chemical shift changes cast light on the mechanism of expansion of the acyl carrier protein core.
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