Abstract
Complete proton NMR assignments have been made for a synthetic 18-amino acid peptide named systemin, which functions as a wound-induced polypeptide hormone in tomato plants, and three of its derivatives. The wild-type peptide and this synthetic homolog have equivalent activities in their functional roles as systemic inducing signals in tomato plants. Proton NMR studies were carried out to characterize the solution properties of systemin. A variety of homonuclear proton NMR experiments at both 500 and 600 MHz were utilized in making these assignments, which have resulted in additional structural information. Whereas these results provide no evidence for persistence of common secondary (helix, sheet) or tertiary structural elements in the systemin polypeptide, there is evidence for two distinct molecular conformations at the carboxy terminus.
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