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Updated: Feb 9, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23
David P Bowles1,2, Alexandar L Hansen3, Calvin A Rhoads2
1Ohio State Biochemistry Program, The Ohio State University, Columbus, OH, 43210, USA.
Abstract:
Er-23 is a small, 51 amino acid, disulfide-rich pheromone protein used for cell signaling by Euplotes raikovi. Ten of the 51 amino acids are cysteine, allowing up to five disulfide bonds. Previous NMR work with Er-23 utilized homologously expressed protein, prohibiting isotopic labeling, and consequently the chemical shift assignments were incomplete. We have expressed uniformly 15N and 13C-labeled Er-23 in an E. coli expression system. Here we report the full backbone and side chain resonance assignments for recombinant Er-23.
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