| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10760132 | Biochemical and Biophysical Research Communications | 2013 | 6 Pages |
Abstract
⺠Cell-free synthesis system suitable for disulfide-containing proteins is proposed. ⺠Disulfide bond formation was facilitated by the use of glutathione buffer. ⺠DsbC catalyzed the efficient shuffling of incorrectly formed disulfide bonds. ⺠Milligram quantities of functional 15N-labeled BPTI and lysozyme C were obtained. ⺠Synthesized proteins were both catalytically functional and properly folded.
Keywords
PEPLysozyme CBPTIMBBRE. coliHSQCDTNBGSSGMWCOGSHscFvnuclear magnetic resonance5,5′-dithiobis-2-nitrobenzoic acidSingle chain FvEscherichia coliStable-isotope labelingNMRCell-free protein synthesisphosphoenolpyruvateLYZbovine pancreatic trypsin inhibitorMonobromobimanemolecular weight cut-offreduced glutathioneoxidized glutathioneheteronuclear single quantum coherence
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Authors
Takayoshi Matsuda, Satoru Watanabe, Takanori Kigawa,