Tandem malonate-based glucosides (TMGs) for membrane protein structural studies

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Tandem malonate-based glucosides (TMGs) for membrane protein structural studies. / Hussain, Hazrat; Mortensen, Jonas S.; Du, Yang; Santillan, Claudia; Ribeiro, Orquidea; Go, Juyeon; Hariharan, Parameswaran; Loland, Claus J.; Guan, Lan; Kobilka, Brian K.; Byrne, Bernadette; Chae, Pil Seok.

In: Scientific Reports, Vol. 7, No. 1, 3963, 2017.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hussain, H, Mortensen, JS, Du, Y, Santillan, C, Ribeiro, O, Go, J, Hariharan, P, Loland, CJ, Guan, L, Kobilka, BK, Byrne, B & Chae, PS 2017, 'Tandem malonate-based glucosides (TMGs) for membrane protein structural studies', Scientific Reports, vol. 7, no. 1, 3963. https://doi.org/10.1038/s41598-017-03809-3

APA

Hussain, H., Mortensen, J. S., Du, Y., Santillan, C., Ribeiro, O., Go, J., Hariharan, P., Loland, C. J., Guan, L., Kobilka, B. K., Byrne, B., & Chae, P. S. (2017). Tandem malonate-based glucosides (TMGs) for membrane protein structural studies. Scientific Reports, 7(1), [3963]. https://doi.org/10.1038/s41598-017-03809-3

Vancouver

Hussain H, Mortensen JS, Du Y, Santillan C, Ribeiro O, Go J et al. Tandem malonate-based glucosides (TMGs) for membrane protein structural studies. Scientific Reports. 2017;7(1). 3963. https://doi.org/10.1038/s41598-017-03809-3

Author

Hussain, Hazrat ; Mortensen, Jonas S. ; Du, Yang ; Santillan, Claudia ; Ribeiro, Orquidea ; Go, Juyeon ; Hariharan, Parameswaran ; Loland, Claus J. ; Guan, Lan ; Kobilka, Brian K. ; Byrne, Bernadette ; Chae, Pil Seok. / Tandem malonate-based glucosides (TMGs) for membrane protein structural studies. In: Scientific Reports. 2017 ; Vol. 7, No. 1.

Bibtex

@article{31a81e5a81464332833f24157a8c068b,
title = "Tandem malonate-based glucosides (TMGs) for membrane protein structural studies",
abstract = "High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research.",
author = "Hazrat Hussain and Mortensen, {Jonas S.} and Yang Du and Claudia Santillan and Orquidea Ribeiro and Juyeon Go and Parameswaran Hariharan and Loland, {Claus J.} and Lan Guan and Kobilka, {Brian K.} and Bernadette Byrne and Chae, {Pil Seok}",
year = "2017",
doi = "10.1038/s41598-017-03809-3",
language = "English",
volume = "7",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Tandem malonate-based glucosides (TMGs) for membrane protein structural studies

AU - Hussain, Hazrat

AU - Mortensen, Jonas S.

AU - Du, Yang

AU - Santillan, Claudia

AU - Ribeiro, Orquidea

AU - Go, Juyeon

AU - Hariharan, Parameswaran

AU - Loland, Claus J.

AU - Guan, Lan

AU - Kobilka, Brian K.

AU - Byrne, Bernadette

AU - Chae, Pil Seok

PY - 2017

Y1 - 2017

N2 - High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research.

AB - High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research.

U2 - 10.1038/s41598-017-03809-3

DO - 10.1038/s41598-017-03809-3

M3 - Journal article

C2 - 28638082

AN - SCOPUS:85021118967

VL - 7

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 3963

ER -

ID: 188448607