1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23 |
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| Authors: | David P. Bowles author-information" >,Alexandar L. Hansen author-information" >,Calvin A. Rhoads,Sidharth Mohan,Chunhua Yuan,Thomas J. Magliery |
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| Affiliation: | 1.Ohio State Biochemistry Program,The Ohio State University,Columbus,USA;2.Department of Chemistry & Biochemistry,The Ohio State University,Columbus,USA;3.Campus Chemical Instrument Center,The Ohio State University,Columbus,USA;4.Biophysics Graduate Program,The Ohio State University,Columbus,USA |
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| 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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