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Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli

Tansila, Natta; Becker, Kristian LU ; Na-Ayudhya, Chartchalerm Isarankura; Prachayasittikul, Virapong and Bülow, Leif LU (2008) In Biotechnology Letters 30(8). p.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.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
metal binding, histidine, protein, green fluorescent, accessible surface area, fluorescent quenching
in
Biotechnology Letters
volume
30
issue
8
pages
1391 - 1396
publisher
Springer
external identifiers
  • wos:000256909200013
  • scopus:45849152604
ISSN
1573-6776
DOI
10.1007/s10529-008-9692-7
language
English
LU publication?
yes
id
b142c2f3-6b7c-41b3-975c-fe92a0c4cca6 (old id 1191181)
date added to LUP
2008-09-08 11:58:04
date last changed
2017-01-01 06:20:21
@article{b142c2f3-6b7c-41b3-975c-fe92a0c4cca6,
  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.},
  author       = {Tansila, Natta and Becker, Kristian and Na-Ayudhya, Chartchalerm Isarankura and Prachayasittikul, Virapong and Bülow, Leif},
  issn         = {1573-6776},
  keyword      = {metal binding,histidine,protein,green fluorescent,accessible surface area,fluorescent quenching},
  language     = {eng},
  number       = {8},
  pages        = {1391--1396},
  publisher    = {Springer},
  series       = {Biotechnology Letters},
  title        = {Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli},
  url          = {http://dx.doi.org/10.1007/s10529-008-9692-7},
  volume       = {30},
  year         = {2008},
}