Publication: Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli
Issued Date
2008-08-01
Resource Type
ISSN
15736776
01415492
01415492
Other identifier(s)
2-s2.0-45849152604
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Biotechnology Letters. Vol.30, No.8 (2008), 1391-1396
Suggested Citation
Natta Tansila, Kristian Becker, Chartchalerm Isarankura Na-Ayudhya, Virapong Prachayasittikul, Leif Bülow Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli. Biotechnology Letters. Vol.30, No.8 (2008), 1391-1396. doi:10.1007/s10529-008-9692-7 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/18879
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli
Other Contributor(s)
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.