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- W2317087631 abstract "Protein immobilization confers the advantages of biological systems to a more chemical setting and has applications in catalysis, sensors, and materials development. While numerous immobilization techniques exist, it is optimal to develop a well-defined and chemically stable methodology to allow for full protein function. This paper describes the utilization of unnatural amino acid technologies to introduce bioorthogonal handles in a site-specific fashion for protein immobilization. To develop this approach a range of solid-supports, organic linkers, and protein immobilization sites have been investigated using a GFP reporter system. Overall, a sepharose resin derivatized with propargyl alcohol has afforded the highest yields of immobilized protein. Moreover, an unnatural amino acid residue protein context has been demonstrated, signifying a necessity to consider the protein site of immobilization. Finally, a resin-conferred stabilization was demonstrated in several organic solvents." @default.
- W2317087631 created "2016-06-24" @default.
- W2317087631 creator A5026822770 @default.
- W2317087631 creator A5060098398 @default.
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- W2317087631 date "2014-10-29" @default.
- W2317087631 modified "2023-09-26" @default.
- W2317087631 title "Site-Specific Protein Immobilization Using Unnatural Amino Acids" @default.
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- W2317087631 doi "https://doi.org/10.1021/bc500443h" @default.
- W2317087631 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25340826" @default.
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