H-1, C-13, and N-15 resonance assignments of ENOD40B, a plant peptide hormone
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ENOD40B, a plant peptide hormone, was doubly labeled with C-13 and N-15 by recombinant production in Escherichia coli. The peptide was prepared by affinity chromatography followed by protease cleavage and reverse-phase chromatography. To elucidate the mode of action against its receptor, sucrose synthase, we proceeded to assign the backbone and side-chain resonances using a set of double and triple resonance experiments. This result will be used to determine the three-dimensional structure of the peptide at its bound state as well as to observe the chemical shift changes upon binding.
Abstract
ENOD40B, a plant peptide hormone, was doubly labeled with C-13 and N-15 by recombinant production in Escherichia coli. The peptide was prepared by affinity chromatography followed by protease cleavage and reverse-phase chromatography. To elucidate the mode of action against its receptor, sucrose synthase, we proceeded to assign the backbone and side-chain resonances using a set of double and triple resonance experiments. This result will be used to determine the three-dimensional structure of the peptide at its bound state as well as to observe the chemical shift changes upon binding.
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