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  Diffusion coefficients and dissociation constants of enhanced green fluorescent protein binding to free standing membranes

Thomas, F. A., Visco, I., Petrasek, Z., Heinemann, F., & Schwille, P. (2015). Diffusion coefficients and dissociation constants of enhanced green fluorescent protein binding to free standing membranes. Data in Brief, 5, 537-541. doi:10.1016/j.dib.2015.10.002.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0029-B204-D Version Permalink: https://hdl.handle.net/21.11116/0000-0007-FE24-3
Genre: Journal Article
Subtitle : Data Article

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 Creators:
Thomas, Franziska A.1, Author           
Visco, Ilaria1, Author           
Petrasek, Zdenek1, Author           
Heinemann, Fabian1, Author           
Schwille, Petra1, Author           
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: -
 Abstract: Recently, a new and versatile assay to determine the partitioning
coef
fi
cient
K
P
as a measure for the af
fi
nity of peripheral membrane
proteins for lipid bilayers was presented in the research article enti-
tled,
“
Introducing a
fl
uorescence-based standard to quantify protein
partitioning into membranes
”
[1]
. Here, the well-characterized bind-
ing of hexahistidine-tag (His
6
) to NTA(Ni) was utilized. Com-
plementarily, this data article reports the average diffusion coef
fi
cient
D
of His
6
-tagged enhanced green
fl
uorescent protein (eGFP-His
6
)and
the
fl
uorescent lipid analog ATTO
‐
647N
‐
DOPE in giant unilamellar
vesicles (GUVs) containing different amounts of NTA(Ni) lipids. In
addition, dissociation constants
K
d
of the NTA(Ni)/eGFP-His
6
system
are reported. Further, a conversion between
K
d
and
K
P
is provided

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Language(s): eng - English
 Dates: 2015
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: Refers to
Franziska A. Thomas, Ilaria Visco, Zdeněk Petrášek, Fabian Heinemann, Petra Schwille
Introducing a fluorescence-based standard to quantify protein partitioning into membranes
Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1848, Issue 11, Part A, November 2015, Pages 2932-2941
 Rev. Type: -
 Identifiers: DOI: 10.1016/j.dib.2015.10.002
 Degree: -

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Title: Data in Brief
  Abbreviation : Data Brief
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Dordrecht : Elsevier
Pages: - Volume / Issue: 5 Sequence Number: - Start / End Page: 537 - 541 Identifier: ISSN: 2352-3409
CoNE: https://pure.mpg.de/cone/journals/resource/2352-3409