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Saravanan Prabhu Nadarajan,카나가벨디판쿠마,서주현,윤형돈 한국생물공학회 2017 Biotechnology and Bioprocess Engineering Vol.22 No.5
In the past decade, numerous studies have been reported that the residue specific incorporation of fluorine containing analogs into protein can enhance the stability of protein. On the other hand, the incorporation of fluoroproline can enhance both stability and refolding rate of recombinant proteins. The objective of this study was to determine the reason behind the enhanced stability and refolding rate of protein by comparing GFP variants containing fluoroproline or hydroxyproline. The fluorine atom of 4-fluoroproline played a significant role in enhancing stability, and Cγ-endo puckering property of (4S)-4-fluoroproline and (4S)-4- hydroxyproline plays a key role in enhancing protein refolding rate.
Engineering lead-sensing GFP through rational designing
Nadarajan, Saravanan Prabhu,Ravikumar, Yuvaraj,Deepankumar, Kanagavel,Lee, Chong-Soon,Yun, Hyungdon The Royal Society of Chemistry 2014 Chemical communications Vol.50 No.100
<P>Lead is one of the most hazardous metals ubiquitous in the environment, causing serious health hazards to organisms. Recently, fluorescent proteins such as GFP and Dsred were utilized for the development of reagent-less rapid metal sensors. Here, we demonstrate the development of a lead-sensing GFP that is highly sensitive to lead at micro molar concentrations.</P> <P>Graphic Abstract</P><P>A lead biosensor (PbGFP) was developed by engineering lead binding site near the chromophore of green fluorescent protein. The specific binding of lead to chromophore of PbGFP resulted in turn-off mechanism. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c4cc07163h'> </P>
Temperature Sensing Using Red Fluorescent Protein
카나가벨디판쿠마,Saravanan Prabhu Nadarajan,배동호,백광현,최권영,윤형돈 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.1
Genetically encoded fluorescent proteins areextensively utilized for labeling and imaging proteins,organelles, cell tissues, and whole organisms. In this study,we explored the feasibility of mRFP1 and its variants formeasuring intracellular temperature. A linear relationshipwas observed between the temperature and fluorescenceintensity of mRFP1 and its variants. Temperature sensitivitiesof E. coli expressing mRFP1, mRFP-P63A and mRFPP63A[(4R)-FP] were -1.27%, -1.26% and -0.77%/°C,respectively. Finally, we demonstrated the potentiality ofmRFP1 and its variants as an in vivo temperature sensor.
카나가벨디판쿠마,Nadarajan Saravanan Prabhu,김준형,윤형돈 한국생물공학회 2017 Biotechnology and Bioprocess Engineering Vol.22 No.3
In 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.