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| Journal Article | PreJuSER-30442 |
; ;
2003
Springer Science + Business Media B.V
Dordrecht [u.a.]
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Please use a persistent id in citations: doi:10.1023/A:1023887412387
Abstract: A widely applicable strategy is presented for efficient and rapid production of small water soluble peptides expressed as fusion proteins with the immunoglobulin-binding domain of streptococcal protein G. A simple extraction and purification scheme that includes a protease cleavage step to release the target peptide is described. The yield of authentic target peptide exceeds 10 mg per liter of culture. Production of U-C-13, N-15 and highly deuterated U-C-13, N-15 isotope labeled peptide is demonstrated for the 11 residue S2 peptide, corresponding to the C-terminus of the alpha-subunit of transducin, and the coiled coil trimerization domain from cartilage matrix protein (CMPcc), respectively. Heteronuclear two-dimensional NMR spectra are used for initial peptide characterization.
Keyword(s): J ; E. coli (auto) ; fusion protein (auto) ; isotope labeling (auto) ; NMR (auto) ; recombinant peptide (auto)
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