http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
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>
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.