Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes

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Standard

Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes. / Mathiasen, Signe; Christensen, Sune M.; Fung, Juan José; Rasmussen, Søren Gøgsig Faarup; Fay, Jonathan F.; Jørgensen, Sune Klamer; Veshaguri, Salome; Farrens, David L.; Kiskowski, Maria; Kobilka, Brian; Stamou, Dimitrios.

I: Nature Methods, Bind 11, 2014, s. 931-934.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Mathiasen, S, Christensen, SM, Fung, JJ, Rasmussen, SGF, Fay, JF, Jørgensen, SK, Veshaguri, S, Farrens, DL, Kiskowski, M, Kobilka, B & Stamou, D 2014, 'Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes', Nature Methods, bind 11, s. 931-934. https://doi.org/10.1038/nmeth.3062

APA

Mathiasen, S., Christensen, S. M., Fung, J. J., Rasmussen, S. G. F., Fay, J. F., Jørgensen, S. K., Veshaguri, S., Farrens, D. L., Kiskowski, M., Kobilka, B., & Stamou, D. (2014). Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes. Nature Methods, 11, 931-934. https://doi.org/10.1038/nmeth.3062

Vancouver

Mathiasen S, Christensen SM, Fung JJ, Rasmussen SGF, Fay JF, Jørgensen SK o.a. Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes. Nature Methods. 2014;11:931-934. https://doi.org/10.1038/nmeth.3062

Author

Mathiasen, Signe ; Christensen, Sune M. ; Fung, Juan José ; Rasmussen, Søren Gøgsig Faarup ; Fay, Jonathan F. ; Jørgensen, Sune Klamer ; Veshaguri, Salome ; Farrens, David L. ; Kiskowski, Maria ; Kobilka, Brian ; Stamou, Dimitrios. / Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes. I: Nature Methods. 2014 ; Bind 11. s. 931-934.

Bibtex

@article{86dfae16bb3b44f5a260c0b2ec8c4855,
title = "Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes",
abstract = "Proteoliposome reconstitution is a standard method to stabilize purified transmembrane proteins in membranes for structural and functional assays. Here we quantified intrareconstitution heterogeneities in single proteoliposomes using fluorescence microscopy. Our results suggest that compositional heterogeneities can severely skew ensemble-average proteoliposome measurements but also enable ultraminiaturized high-content screens. We took advantage of this screening capability to map the oligomerization energy of the β2-adrenergic receptor using ∼10(9)-fold less protein than conventional assays.",
author = "Signe Mathiasen and Christensen, {Sune M.} and Fung, {Juan Jos{\'e}} and Rasmussen, {S{\o}ren G{\o}gsig Faarup} and Fay, {Jonathan F.} and J{\o}rgensen, {Sune Klamer} and Salome Veshaguri and Farrens, {David L.} and Maria Kiskowski and Brian Kobilka and Dimitrios Stamou",
year = "2014",
doi = "10.1038/nmeth.3062",
language = "English",
volume = "11",
pages = "931--934",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes

AU - Mathiasen, Signe

AU - Christensen, Sune M.

AU - Fung, Juan José

AU - Rasmussen, Søren Gøgsig Faarup

AU - Fay, Jonathan F.

AU - Jørgensen, Sune Klamer

AU - Veshaguri, Salome

AU - Farrens, David L.

AU - Kiskowski, Maria

AU - Kobilka, Brian

AU - Stamou, Dimitrios

PY - 2014

Y1 - 2014

N2 - Proteoliposome reconstitution is a standard method to stabilize purified transmembrane proteins in membranes for structural and functional assays. Here we quantified intrareconstitution heterogeneities in single proteoliposomes using fluorescence microscopy. Our results suggest that compositional heterogeneities can severely skew ensemble-average proteoliposome measurements but also enable ultraminiaturized high-content screens. We took advantage of this screening capability to map the oligomerization energy of the β2-adrenergic receptor using ∼10(9)-fold less protein than conventional assays.

AB - Proteoliposome reconstitution is a standard method to stabilize purified transmembrane proteins in membranes for structural and functional assays. Here we quantified intrareconstitution heterogeneities in single proteoliposomes using fluorescence microscopy. Our results suggest that compositional heterogeneities can severely skew ensemble-average proteoliposome measurements but also enable ultraminiaturized high-content screens. We took advantage of this screening capability to map the oligomerization energy of the β2-adrenergic receptor using ∼10(9)-fold less protein than conventional assays.

U2 - 10.1038/nmeth.3062

DO - 10.1038/nmeth.3062

M3 - Journal article

C2 - 25086504

VL - 11

SP - 931

EP - 934

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

ER -

ID: 120586968