1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23
| Autor: | Chunhua Yuan, David Bowles, Calvin A. Rhoads, Thomas J. Magliery, Sidharth Mohan, Alexandar L. Hansen |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Cell signaling Stereochemistry Resonance (chemistry) Biochemistry Amino acid law.invention Isotopic labeling 03 medical and health sciences 030104 developmental biology chemistry Structural Biology law Side chain Recombinant DNA Euplotes raikovi Cysteine |
| Zdroj: | Biomolecular NMR Assignments. 12:291-295 |
| ISSN: | 1874-270X 1874-2718 |
| DOI: | 10.1007/s12104-018-9825-4 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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