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Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study. / Chae, Pil Seok; Rana, Rohini R; Gotfryd, Kamil; Rasmussen, Søren G F; Kruse, Andrew C; Cho, Kyung Ho; Capaldi, Stefano; Carlsson, Emil; Kobilka, Brian; Loland, Claus J; Gether, Ulrik; Banerjee, Surajit; Byrne, Bernadette; Lee, John K; Gellman, Samuel H.
In:
Chemical communications (Cambridge, England), Vol. 49, No. 23, 21.03.2013, p. 2287-9.
Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
Chae, PS, Rana, RR, Gotfryd, K
, Rasmussen, SGF, Kruse, AC, Cho, KH, Capaldi, S, Carlsson, E, Kobilka, B
, Loland, CJ, Gether, U, Banerjee, S, Byrne, B, Lee, JK & Gellman, SH 2013, '
Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study',
Chemical communications (Cambridge, England), vol. 49, no. 23, pp. 2287-9.
https://doi.org/10.1039/c2cc36844gAPA
Chae, P. S., Rana, R. R., Gotfryd, K.
, Rasmussen, S. G. F., Kruse, A. C., Cho, K. H., Capaldi, S., Carlsson, E., Kobilka, B.
, Loland, C. J., Gether, U., Banerjee, S., Byrne, B., Lee, J. K., & Gellman, S. H. (2013).
Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study.
Chemical communications (Cambridge, England),
49(23), 2287-9.
https://doi.org/10.1039/c2cc36844gVancouver
Chae PS, Rana RR, Gotfryd K
, Rasmussen SGF, Kruse AC, Cho KH et al.
Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study.
Chemical communications (Cambridge, England). 2013 Mar 21;49(23):2287-9.
https://doi.org/10.1039/c2cc36844gAuthor
Chae, Pil Seok ; Rana, Rohini R ; Gotfryd, Kamil ; Rasmussen, Søren G F ; Kruse, Andrew C ; Cho, Kyung Ho ; Capaldi, Stefano ; Carlsson, Emil ; Kobilka, Brian ; Loland, Claus J ; Gether, Ulrik ; Banerjee, Surajit ; Byrne, Bernadette ; Lee, John K ; Gellman, Samuel H. / Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study. In: Chemical communications (Cambridge, England). 2013 ; Vol. 49, No. 23. pp. 2287-9.
Bibtex
@article{2c47a3fa9f74423fbbce424060343d2e,
title = "Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study",
abstract = "The development of a new class of surfactants for membrane protein manipulation, {"}GNG amphiphiles{"}, is reported. These amphiphiles display promising behavior for membrane proteins, as demonstrated recently by the high resolution structure of a sodium-pumping pyrophosphatase reported by Kellosalo et al. (Science, 2012, 337, 473).",
author = "Chae, {Pil Seok} and Rana, {Rohini R} and Kamil Gotfryd and Rasmussen, {S{\o}ren G F} and Kruse, {Andrew C} and Cho, {Kyung Ho} and Stefano Capaldi and Emil Carlsson and Brian Kobilka and Loland, {Claus J} and Ulrik Gether and Surajit Banerjee and Bernadette Byrne and Lee, {John K} and Gellman, {Samuel H}",
year = "2013",
month = mar,
day = "21",
doi = "10.1039/c2cc36844g",
language = "English",
volume = "49",
pages = "2287--9",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "23",
}
RIS
TY - JOUR
T1 - Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study
AU - Chae, Pil Seok
AU - Rana, Rohini R
AU - Gotfryd, Kamil
AU - Rasmussen, Søren G F
AU - Kruse, Andrew C
AU - Cho, Kyung Ho
AU - Capaldi, Stefano
AU - Carlsson, Emil
AU - Kobilka, Brian
AU - Loland, Claus J
AU - Gether, Ulrik
AU - Banerjee, Surajit
AU - Byrne, Bernadette
AU - Lee, John K
AU - Gellman, Samuel H
PY - 2013/3/21
Y1 - 2013/3/21
N2 - The development of a new class of surfactants for membrane protein manipulation, "GNG amphiphiles", is reported. These amphiphiles display promising behavior for membrane proteins, as demonstrated recently by the high resolution structure of a sodium-pumping pyrophosphatase reported by Kellosalo et al. (Science, 2012, 337, 473).
AB - The development of a new class of surfactants for membrane protein manipulation, "GNG amphiphiles", is reported. These amphiphiles display promising behavior for membrane proteins, as demonstrated recently by the high resolution structure of a sodium-pumping pyrophosphatase reported by Kellosalo et al. (Science, 2012, 337, 473).
U2 - 10.1039/c2cc36844g
DO - 10.1039/c2cc36844g
M3 - Journal article
C2 - 23165475
VL - 49
SP - 2287
EP - 2289
JO - Chemical Communications
JF - Chemical Communications
SN - 1359-7345
IS - 23
ER -
