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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/18879
Title: Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli
Authors: Natta Tansila
Kristian Becker
Chartchalerm Isarankura Na-Ayudhya
Virapong Prachayasittikul
Leif Bülow
Mahidol University
Lunds Universitet
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Aug-2008
Citation: Biotechnology Letters. Vol.30, No.8 (2008), 1391-1396
Abstract: Green fluorescent protein (GFP) is frequently utilized for metal ion detection and quantification. To improve the metal binding potential of GFP, three residues (N146, F165, and L201) were substituted to histidines. Each variant responded differently upon interaction with metal ions. More than 80% of N146H, having the most accessible surface area, could bind to immobilized metal ions. However, only F165H exhibited significant differences in quenching by soluble metal ions (22% fluorescence decrease) in comparison with the template protein (12%). These findings can be utilized for designing GFP variants for metal binding and sensor applications. © 2008 Springer Science+Business Media B.V.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=45849152604&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/18879
ISSN: 15736776
01415492
Appears in Collections:Scopus 2006-2010

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