dc.contributor.authorDeepankumar, Kanagavel
dc.contributor.authorPrabhu, Nadarajan Saravanan
dc.contributor.authorKim, June-Hyung
dc.contributor.authorYun, Hyungdon
dc.identifier.citationDeepankumar, K., Prabhu, N. S., Kim, J.-H., & Yun, H. (2017). Protein engineering for covalent immobilization and enhanced stability through incorporation of multiple noncanonical amino acids. Biotechnology and Bioprocess Engineering, 22(3), 248-255.en_US
dc.description.abstractIn this study, we demonstrate the application of multiple functional properties of proteins generated through coupling of residue-specific and site-specific incorporation method. With green fluorescent protein (GFP) as a model protein, we constructed multifunctional GFP through sitespecific incorporation of L-3,4-dihydroxyphenylalanine (DOPA) and residue-specific incorporation of (2S, 4S)-4- fluoroproline (4S-FP) or L-homopropargylglycine (hpg). Fluorescence analysis revealed a conjugation efficiency of approximately 20% for conjugation of DOPA-containing variants GFPdopa, GFPdp[4S-FP], and GFPdphpg onto chitosan. While incorporation of 4S-FP improved protein folding and stability, hpg incorporation into GFP allowed conjugation with fluorescent dye/polyethylene glycol (PEG). In addition, the modification of GFPhpg and GFPdphpg with PEG through Cu(I)-catalyzed click reaction increased protein thermal stability by about two-fold of the wild-type GFP.en_US
dc.relation.ispartofseriesBiotechnology and Bioprocess Engineeringen_US
dc.rights© 2017 The Korean Society for Biotechnology and Bioengineering and Springeren_US
dc.subjectMultiple noncanonical amino acidsen_US
dc.titleProtein engineering for covalent immobilization and enhanced stability through incorporation of multiple noncanonical amino acidsen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Materials Science and Engineeringen_US

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