Novel Tripod Amphiphiles for Membrane Protein Analysis

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

Standard

Novel Tripod Amphiphiles for Membrane Protein Analysis. / Chae, Pil Seok; Kruse, Andrew C; Gotfryd, Kamil; Rana, Rohini R; Cho, Kyung Ho; Rasmussen, Søren G F; Bae, Hyoung Eun; Chandra, Richa; Gether, Ulrik; Guan, Lan; Kobilka, Brian K; Loland, Claus J; Byrne, Bernadette; Gellman, Samuel H.

In: Chemistry: A European Journal, Vol. 19, No. 46, 02.10.2013.

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

Harvard

Chae, PS, Kruse, AC, Gotfryd, K, Rana, RR, Cho, KH, Rasmussen, SGF, Bae, HE, Chandra, R, Gether, U, Guan, L, Kobilka, BK, Loland, CJ, Byrne, B & Gellman, SH 2013, 'Novel Tripod Amphiphiles for Membrane Protein Analysis', Chemistry: A European Journal, vol. 19, no. 46. https://doi.org/10.1002/chem.201301423

APA

Chae, P. S., Kruse, A. C., Gotfryd, K., Rana, R. R., Cho, K. H., Rasmussen, S. G. F., Bae, H. E., Chandra, R., Gether, U., Guan, L., Kobilka, B. K., Loland, C. J., Byrne, B., & Gellman, S. H. (2013). Novel Tripod Amphiphiles for Membrane Protein Analysis. Chemistry: A European Journal, 19(46). https://doi.org/10.1002/chem.201301423

Vancouver

Chae PS, Kruse AC, Gotfryd K, Rana RR, Cho KH, Rasmussen SGF et al. Novel Tripod Amphiphiles for Membrane Protein Analysis. Chemistry: A European Journal. 2013 Oct 2;19(46). https://doi.org/10.1002/chem.201301423

Author

Chae, Pil Seok ; Kruse, Andrew C ; Gotfryd, Kamil ; Rana, Rohini R ; Cho, Kyung Ho ; Rasmussen, Søren G F ; Bae, Hyoung Eun ; Chandra, Richa ; Gether, Ulrik ; Guan, Lan ; Kobilka, Brian K ; Loland, Claus J ; Byrne, Bernadette ; Gellman, Samuel H. / Novel Tripod Amphiphiles for Membrane Protein Analysis. In: Chemistry: A European Journal. 2013 ; Vol. 19, No. 46.

Bibtex

@article{a1680cdbc45742c5a37355fb343a76da,

title = "Novel Tripod Amphiphiles for Membrane Protein Analysis",

abstract = "Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.",

author = "Chae, {Pil Seok} and Kruse, {Andrew C} and Kamil Gotfryd and Rana, {Rohini R} and Cho, {Kyung Ho} and Rasmussen, {S{\o}ren G F} and Bae, {Hyoung Eun} and Richa Chandra and Ulrik Gether and Lan Guan and Kobilka, {Brian K} and Loland, {Claus J} and Bernadette Byrne and Gellman, {Samuel H}",

note = "Copyright {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

year = "2013",

month = oct,

day = "2",

doi = "10.1002/chem.201301423",

language = "English",

volume = "19",

journal = "Chemistry: A European Journal",

issn = "0947-6539",

publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",

number = "46",

}

RIS

TY - JOUR

T1 - Novel Tripod Amphiphiles for Membrane Protein Analysis

AU - Chae, Pil Seok

AU - Kruse, Andrew C

AU - Gotfryd, Kamil

AU - Rana, Rohini R

AU - Cho, Kyung Ho

AU - Rasmussen, Søren G F

AU - Bae, Hyoung Eun

AU - Chandra, Richa

AU - Gether, Ulrik

AU - Guan, Lan

AU - Kobilka, Brian K

AU - Loland, Claus J

AU - Byrne, Bernadette

AU - Gellman, Samuel H

PY - 2013/10/2

Y1 - 2013/10/2

N2 - Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.

AB - Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.

U2 - 10.1002/chem.201301423

DO - 10.1002/chem.201301423

M3 - Journal article

C2 - 24123610

VL - 19

JO - Chemistry: A European Journal

JF - Chemistry: A European Journal

SN - 0947-6539

IS - 46

ER -

ID: 54574489

Forskning