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A Combinatorial Strategy for HRV 3C Protease Engineering to Achieve the N-terminal Free Cleavage

2024-01-05

Abstract excerpt

Human rhinovirus 3C protease (HRV 3C-P) has a high specificity against the substrate of LEVLFQ↓G at P1’ site, which plays an important role in biotechnology and academia as a fusion tag removal tool. However, a non-ignorable limitation is that an extra residue of Gly would remain at the N terminus of the recombinant target protein after cleavage with HRV 3C-P, thus potentially causing protein mis-functionality or...

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Literature Corpus work
4da46e46-09f6-5d4d-85bc-942d20095873
DOI
10.1101/2024.01.05.574269
Open publication

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A Combinatorial Strategy for HRV 3C Protease Engineering to Achieve the N-terminal Free CleavageDOI 10.1101/2024.01.05.574269
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