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- W2984714480 abstract "We have engineered the substrate specificity of chymotrypsin to cleave after Asn by high-throughput screening of large libraries created by comprehensive remodeling of the substrate binding pocket. The engineered variant (chymotrypsiN, ChyB-Asn) demonstrated an altered substrate specificity with an expanded preference for Asn-containing substrates. We confirmed that protein engineering did not compromise the stability of the enzyme by biophysical characterization. Comparison of wild-type ChyB and ChyB-Asn in profiling lysates of HEK293 cells demonstrated both qualitative and quantitative differences in the nature of the peptides and proteins identified by liquid chromatography and tandem mass spectrometry. ChyB-Asn enabled the identification of partially glycosylated Asn sites within a model glycoprotein and in the extracellular proteome of Jurkat T cells. ChymotrypsiN is a valuable addition to the toolkit of proteases to aid the mapping of N-linked glycosylation sites within proteins and proteomes." @default.
- W2984714480 created "2019-11-22" @default.
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- W2984714480 date "2019-11-11" @default.
- W2984714480 modified "2023-10-18" @default.
- W2984714480 title "Engineered ChymotrypsiN for Mass Spectrometry-Based Detection of Protein Glycosylation" @default.
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- W2984714480 doi "https://doi.org/10.1021/acschembio.9b00506" @default.
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