Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level

Research output: Contribution to journal › Review › Research › peer-review

Standard

Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level. / Veit, Sarina; Paweletz, Laura Charlotte; Pomorski, Thomas Guenther.

In: Biological Chemistry, Vol. 404, No. 7, 2023.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Veit, S, Paweletz, LC & Pomorski, TG 2023, 'Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level', Biological Chemistry, vol. 404, no. 7. https://doi.org/10.1515/hsz-2022-0325

APA

Veit, S., Paweletz, L. C., & Pomorski, T. G. (2023). Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level. Biological Chemistry, 404(7). https://doi.org/10.1515/hsz-2022-0325

Vancouver

Veit S, Paweletz LC, Pomorski TG. Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level. Biological Chemistry. 2023;404(7). https://doi.org/10.1515/hsz-2022-0325

Author

Veit, Sarina ; Paweletz, Laura Charlotte ; Pomorski, Thomas Guenther. / Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level. In: Biological Chemistry. 2023 ; Vol. 404, No. 7.

Bibtex

@article{26376a690edb487c98e569442bb6f76c,
title = "Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level",
abstract = "Reconstitution of membrane proteins into liposomal membranes represents a key technique in enabling functional analysis under well-defined conditions. In this review, we provide a brief introduction to selected methods that have been developed to determine membrane protein orientation after reconstitution in liposomes, including approaches based on proteolytic digestion with proteases, site-specific labeling, fluorescence quenching and activity assays. In addition, we briefly highlight new strategies based on single vesicle analysis to address the problem of sample heterogeneity.",
keywords = "membrane protein, protease, proteoliposome, quencher, reconstitution, single vesicle, ORIENTED INSERTION, LIPID-COMPOSITION, FUSION PROTEINS, PH CHANGES, BACTERIORHODOPSIN, SITE, TRANSLOCATION, MECHANISMS, MOLECULES, TRANSPORT",
author = "Sarina Veit and Paweletz, {Laura Charlotte} and Pomorski, {Thomas Guenther}",
year = "2023",
doi = "10.1515/hsz-2022-0325",
language = "English",
volume = "404",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "De Gruyter",
number = "7",

}

RIS

TY - JOUR

T1 - Determination of membrane protein orientation upon liposomal reconstitution down to the single vesicle level

AU - Veit, Sarina

AU - Paweletz, Laura Charlotte

AU - Pomorski, Thomas Guenther

PY - 2023

Y1 - 2023

N2 - Reconstitution of membrane proteins into liposomal membranes represents a key technique in enabling functional analysis under well-defined conditions. In this review, we provide a brief introduction to selected methods that have been developed to determine membrane protein orientation after reconstitution in liposomes, including approaches based on proteolytic digestion with proteases, site-specific labeling, fluorescence quenching and activity assays. In addition, we briefly highlight new strategies based on single vesicle analysis to address the problem of sample heterogeneity.

AB - Reconstitution of membrane proteins into liposomal membranes represents a key technique in enabling functional analysis under well-defined conditions. In this review, we provide a brief introduction to selected methods that have been developed to determine membrane protein orientation after reconstitution in liposomes, including approaches based on proteolytic digestion with proteases, site-specific labeling, fluorescence quenching and activity assays. In addition, we briefly highlight new strategies based on single vesicle analysis to address the problem of sample heterogeneity.

KW - membrane protein

KW - protease

KW - proteoliposome

KW - quencher

KW - reconstitution

KW - single vesicle

KW - ORIENTED INSERTION

KW - LIPID-COMPOSITION

KW - FUSION PROTEINS

KW - PH CHANGES

KW - BACTERIORHODOPSIN

KW - SITE

KW - TRANSLOCATION

KW - MECHANISMS

KW - MOLECULES

KW - TRANSPORT

U2 - 10.1515/hsz-2022-0325

DO - 10.1515/hsz-2022-0325

M3 - Review

C2 - 36857289

VL - 404

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 7

ER -

ID: 339139966