A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes

Wei Zhang; Miho Suzuki; Yoichiro Ito; Kenneth T. Douglas

doi:10.1246/cl.2005.766

A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes

Wei Zhang, Miho Suzuki, Yoichiro Ito, Kenneth T. Douglas

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

Abstract

The mixed disulfide of a Green-Fluorescent Protein with an Alexa 532 fluorescent label showed FRET, with quenching of the GFP emission. Reductive cleavage of this disulfide bond destroyed the FRET, giving a change in the ratios of fluorescence intensity at the wavelengths corresponding to the GFP and the Alexa dye. Cleavage by glutathione (second order rate constant at pH 7.4 was 1.18 ± 0.02 × 10 2 Min -1 min -1) was faster than for sodium cyanoborohydride. Copyright © 2005 The Chemical Society of Japan.

Original language	English
Pages (from-to)	766-767
Number of pages	1
Journal	Chemistry Letters
Volume	34
Issue number	6
DOIs	https://doi.org/10.1246/cl.2005.766
Publication status	Published - 5 Jun 2005

Access to Document

10.1246/cl.2005.766

Cite this

@article{fc6c96227e17478c8674608db5cf0df6,

title = "A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes",

abstract = "The mixed disulfide of a Green-Fluorescent Protein with an Alexa 532 fluorescent label showed FRET, with quenching of the GFP emission. Reductive cleavage of this disulfide bond destroyed the FRET, giving a change in the ratios of fluorescence intensity at the wavelengths corresponding to the GFP and the Alexa dye. Cleavage by glutathione (second order rate constant at pH 7.4 was 1.18 ± 0.02 × 10 2 Min -1 min -1) was faster than for sodium cyanoborohydride. Copyright {\textcopyright} 2005 The Chemical Society of Japan.",

author = "Wei Zhang and Miho Suzuki and Yoichiro Ito and Douglas, {Kenneth T.}",

year = "2005",

month = jun,

day = "5",

doi = "10.1246/cl.2005.766",

language = "English",

volume = "34",

pages = "766--767",

journal = "Chemistry Letters",

issn = "1348-0715",

publisher = "Oxford University Press",

number = "6",

}

TY - JOUR

T1 - A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes

AU - Zhang, Wei

AU - Suzuki, Miho

AU - Ito, Yoichiro

AU - Douglas, Kenneth T.

PY - 2005/6/5

Y1 - 2005/6/5

N2 - The mixed disulfide of a Green-Fluorescent Protein with an Alexa 532 fluorescent label showed FRET, with quenching of the GFP emission. Reductive cleavage of this disulfide bond destroyed the FRET, giving a change in the ratios of fluorescence intensity at the wavelengths corresponding to the GFP and the Alexa dye. Cleavage by glutathione (second order rate constant at pH 7.4 was 1.18 ± 0.02 × 10 2 Min -1 min -1) was faster than for sodium cyanoborohydride. Copyright © 2005 The Chemical Society of Japan.

AB - The mixed disulfide of a Green-Fluorescent Protein with an Alexa 532 fluorescent label showed FRET, with quenching of the GFP emission. Reductive cleavage of this disulfide bond destroyed the FRET, giving a change in the ratios of fluorescence intensity at the wavelengths corresponding to the GFP and the Alexa dye. Cleavage by glutathione (second order rate constant at pH 7.4 was 1.18 ± 0.02 × 10 2 Min -1 min -1) was faster than for sodium cyanoborohydride. Copyright © 2005 The Chemical Society of Japan.

U2 - 10.1246/cl.2005.766

DO - 10.1246/cl.2005.766

M3 - Article

SN - 1348-0715

VL - 34

SP - 766

EP - 767

JO - Chemistry Letters

JF - Chemistry Letters

IS - 6

ER -

A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes

Abstract

Access to Document

Fingerprint

Cite this