Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

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

Standard

Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. / Chae, Pil Seok; Rasmussen, Søren G F; Rana, Rohini R; Gotfryd, Kamil; Chandra, Richa; Goren, Michael A; Kruse, Andrew C; Nurva, Shailika; Løland, Claus Juul; Pierre, Yves; Drew, David; Popot, Jean-Luc; Picot, Daniel; Fox, Brian G; Guan, Lan; Gether, Ulrik; Byrne, Bernadette; Kobilka, Brian; Gellman, Samuel H.

In: Nature Methods, Vol. 7, 2010, p. 1003-8.

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

Harvard

Chae, PS, Rasmussen, SGF, Rana, RR, Gotfryd, K, Chandra, R, Goren, MA, Kruse, AC, Nurva, S, Løland, CJ, Pierre, Y, Drew, D, Popot, J-L, Picot, D, Fox, BG, Guan, L, Gether, U, Byrne, B, Kobilka, B & Gellman, SH 2010, 'Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins', Nature Methods, vol. 7, pp. 1003-8. https://doi.org/10.1038/nmeth.1526

APA

Chae, P. S., Rasmussen, S. G. F., Rana, R. R., Gotfryd, K., Chandra, R., Goren, M. A., Kruse, A. C., Nurva, S., Løland, C. J., Pierre, Y., Drew, D., Popot, J-L., Picot, D., Fox, B. G., Guan, L., Gether, U., Byrne, B., Kobilka, B., & Gellman, S. H. (2010). Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nature Methods, 7, 1003-8. https://doi.org/10.1038/nmeth.1526

Vancouver

Chae PS, Rasmussen SGF, Rana RR, Gotfryd K, Chandra R, Goren MA et al. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. Nature Methods. 2010;7:1003-8. https://doi.org/10.1038/nmeth.1526

Author

Chae, Pil Seok ; Rasmussen, Søren G F ; Rana, Rohini R ; Gotfryd, Kamil ; Chandra, Richa ; Goren, Michael A ; Kruse, Andrew C ; Nurva, Shailika ; Løland, Claus Juul ; Pierre, Yves ; Drew, David ; Popot, Jean-Luc ; Picot, Daniel ; Fox, Brian G ; Guan, Lan ; Gether, Ulrik ; Byrne, Bernadette ; Kobilka, Brian ; Gellman, Samuel H. / Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins. In: Nature Methods. 2010 ; Vol. 7. pp. 1003-8.

Bibtex

@article{31747640ecc611dfb6d2000ea68e967b,
title = "Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins",
abstract = "The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.",
author = "Chae, {Pil Seok} and Rasmussen, {S{\o}ren G F} and Rana, {Rohini R} and Kamil Gotfryd and Richa Chandra and Goren, {Michael A} and Kruse, {Andrew C} and Shailika Nurva and L{\o}land, {Claus Juul} and Yves Pierre and David Drew and Jean-Luc Popot and Daniel Picot and Fox, {Brian G} and Lan Guan and Ulrik Gether and Bernadette Byrne and Brian Kobilka and Gellman, {Samuel H}",
year = "2010",
doi = "10.1038/nmeth.1526",
language = "English",
volume = "7",
pages = "1003--8",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

AU - Chae, Pil Seok

AU - Rasmussen, Søren G F

AU - Rana, Rohini R

AU - Gotfryd, Kamil

AU - Chandra, Richa

AU - Goren, Michael A

AU - Kruse, Andrew C

AU - Nurva, Shailika

AU - Løland, Claus Juul

AU - Pierre, Yves

AU - Drew, David

AU - Popot, Jean-Luc

AU - Picot, Daniel

AU - Fox, Brian G

AU - Guan, Lan

AU - Gether, Ulrik

AU - Byrne, Bernadette

AU - Kobilka, Brian

AU - Gellman, Samuel H

PY - 2010

Y1 - 2010

N2 - The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.

AB - The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.

U2 - 10.1038/nmeth.1526

DO - 10.1038/nmeth.1526

M3 - Journal article

C2 - 21037590

VL - 7

SP - 1003

EP - 1008

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

ER -

ID: 23065334