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

Protein Engineering

Onderzoeksoutput: Bijdrage aan tijdschrift › Tijdschriftartikel › Academic › peer review

101 Citaten (Scopus)

6 Downloads (Pure)

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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.

Originele taal-2	Engels
Pagina's (van-tot)	3494-3495
Tijdschrift	Journal of the American Chemical Society
Volume	129
Nummer van het tijdschrift	12
DOI's	https://doi.org/10.1021/ja069105d
Status	Gepubliceerd - 2007

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10.1021/ja069105d

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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",

doi = "10.1021/ja069105d",

language = "English",

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, Nr. 12, 2007, blz. 3494-3495.

Onderzoeksoutput: Bijdrage aan tijdschrift › Tijdschriftartikel › Academic › peer review

TY - JOUR

T1 - Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range

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

Y1 - 2007

N2 - 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.

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

SN - 0002-7863

VL - 129

SP - 3494

EP - 3495

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 12

ER -

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

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