Abstract
The EMB-1 protein is a highly hydrophilic protein of unknown function that accumulates in embryos of carrot before seed desiccation. To investigate the structure of this protein, it was expressed in E. coli, and purified to near homogeneity by Q-Sepharose anion exchange chromatography and ultrafiltration. The purified protein was characterized by 1H nuclear magnetic resonance (NMR) spectroscopy under both aqueous conditions and conditions simulating desiccation. The NMR results reveal poor chemical shift dispersion, rapid chemical exchange of the amide backbone protons, unexpectedly narrow linewidths and the general absence of nuclear Overhauser effects. Together, these results indicate the EMB-1 protein has no defined secondary or tertiary structure in solution and the polypeptide backbone of the EMB-1 protein is flexible on a sub-nanosecond time scale.
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