Nanoscale high-content analysis using compositional heterogeneities of single proteoliposomes

被引：0

作者：

Mathiasen S. ^{[1
,2
,3
]}

Christensen S.M. ^{[1
,2
,3
]}

Fung J.J. ^{[4
,8
]}

Rasmussen S.G.F. ^{[4
,5
]}

Fay J.F. ^{[6
]}

Jorgensen S.K. ^{[1
,2
,3
]}

Veshaguri S. ^{[1
,2
,3
]}

Farrens D.L. ^{[6
]}

Kiskowski M. ^{[7
]}

Kobilka B. ^{[4
]}

Stamou D. ^{[1
,2
,3
]}

机构：

[1] Department of Chemistry, University of Copenhagen, Copenhagen

[2] Nano-Science Center, University of Copenhagen, Copenhagen

[3] Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen

[4] Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Palo Alto, CA

[5] Department of Neuroscience and Pharmacology, University of Copenhagen, Copenhagen

[6] Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR

[7] Department of Mathematics and Statistics, University of South Alabama, Mobile, AL

[8] ProNovus Bioscience, Mountain View, CA

来源：

Nature Methods | 2014年 / 11卷 / 9期

关键词：

D O I：

10.1038/nmeth.3062

中图分类号：

学科分类号：

摘要：

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 b2-adrenergic receptor using ~109-fold less protein than conventional assays.

引用

页码：931 / 934

页数：3

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