Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range

E.M.W.M. Dongen, van; T.H. Evers; L.M. Dekkers; E.W. Meijer; L.W.J. Klomp; M. Merkx

doi:10.1021/ja069105d

Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range

E.M.W.M. Dongen, van, T.H. Evers, L.M. Dekkers, E.W. Meijer, L.W.J. Klomp, M. Merkx

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

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Abstract

Ratiometric fluorescent sensor proteins with a very high and tunable affinity for Zn(II) were created by connecting two fluorescently labeled metal binding domains, CFP-Atox1 and WD4-YFP, using a series of flexible peptide linkers. A simple random-coil model describing the conformational distribution of the linker allowed a quant. understanding of the effect of the linker length on both the change in emission ratio and the Zn(II) affinity.

Original language	English
Pages (from-to)	3494-3495
Journal	Journal of the American Chemical Society
Volume	129
Issue number	12
DOIs	https://doi.org/10.1021/ja069105d
Publication status	Published - 2007

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10.1021/ja069105d

Cite this

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title = "Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range",

abstract = "Ratiometric fluorescent sensor proteins with a very high and tunable affinity for Zn(II) were created by connecting two fluorescently labeled metal binding domains, CFP-Atox1 and WD4-YFP, using a series of flexible peptide linkers. A simple random-coil model describing the conformational distribution of the linker allowed a quant. understanding of the effect of the linker length on both the change in emission ratio and the Zn(II) affinity.",

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year = "2007",

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volume = "129",

pages = "3494--3495",

journal = "Journal of the American Chemical Society",

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publisher = "American Chemical Society",

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Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range. / Dongen, van, E.M.W.M.; Evers, T.H.; Dekkers, L.M. et al.

In: Journal of the American Chemical Society, Vol. 129, No. 12, 2007, p. 3494-3495.

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

TY - JOUR

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AU - Dongen, van, E.M.W.M.

AU - Evers, T.H.

AU - Dekkers, L.M.

AU - Meijer, E.W.

AU - Klomp, L.W.J.

AU - Merkx, M.

PY - 2007

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AB - Ratiometric fluorescent sensor proteins with a very high and tunable affinity for Zn(II) were created by connecting two fluorescently labeled metal binding domains, CFP-Atox1 and WD4-YFP, using a series of flexible peptide linkers. A simple random-coil model describing the conformational distribution of the linker allowed a quant. understanding of the effect of the linker length on both the change in emission ratio and the Zn(II) affinity.

U2 - 10.1021/ja069105d

DO - 10.1021/ja069105d

M3 - Article

C2 - 17335212

VL - 129

SP - 3494

EP - 3495

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

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