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

Natta Tansila; Kristian Becker; Chartchalerm Isarankura Na-Ayudhya; Virapong Prachayasittikul; Leif Bülow

doi:10.1007/s10529-008-9692-7

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

Natta Tansila, Kristian Becker, Chartchalerm Isarankura Na-Ayudhya, Virapong Prachayasittikul, Leif Bülow

Pure and Applied Biochemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	1391-1396
Journal	Biotechnology Letters
Volume	30
Issue number	8
DOIs	https://doi.org/10.1007/s10529-008-9692-7
Publication status	Published - 2008

Subject classification (UKÄ)

Biological Sciences

Free keywords

metal binding
histidine
protein
green fluorescent
accessible surface area
fluorescent quenching

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10.1007/s10529-008-9692-7

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title = "Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli",

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.",

keywords = "metal binding, histidine, protein, green fluorescent, accessible surface area, fluorescent quenching",

author = "Natta Tansila and Kristian Becker and Na-Ayudhya, {Chartchalerm Isarankura} and Virapong Prachayasittikul and Leif B{\"u}low",

year = "2008",

doi = "10.1007/s10529-008-9692-7",

language = "English",

volume = "30",

pages = "1391--1396",

journal = "Biotechnology Letters",

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T1 - Metal ion accessibility of histidine-modified superfolder green fluorescent protein expressed in Escherichia coli

AU - Tansila, Natta

AU - Becker, Kristian

AU - Na-Ayudhya, Chartchalerm Isarankura

AU - Prachayasittikul, Virapong

AU - Bülow, Leif

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - metal binding

KW - histidine

KW - protein

KW - green fluorescent

KW - accessible surface area

KW - fluorescent quenching

U2 - 10.1007/s10529-008-9692-7

DO - 10.1007/s10529-008-9692-7

M3 - Article

C2 - 18338218

SN - 1573-6776

VL - 30

SP - 1391

EP - 1396

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 8

ER -

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

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Subject classification (UKÄ)

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