Abstract
Proteins which are found embedded in membranes can usually only be purified and studied from the point of view of structure by dissolving them in detergents. The structure of the resulting mixed protein-detergent complexes are poorly understood. An important method for studying them is through neutron diffraction of the crystalline complexes. This allows us to understand better how the proteins behave in the natural membrane as well as allowing us to visualize and hopefully improve the crystallisation process. Studies on the pore-forming protein porin using data collected on the diffractometer DB21 are described. (author). 4 refs.
Timmins, P A;
Penel, S;
[1]
Pebay-Peyroula, E
[2]
- Institut Max von Laue - Paul Langevin (ILL), 38 - Grenoble (France)
- IBS- UJF Grenoble (France)
Citation Formats
Timmins, P A, Penel, S, and Pebay-Peyroula, E.
The study of membrane-protein /detergent interactions by neutron crystallography.
France: N. p.,
1997.
Web.
Timmins, P A, Penel, S, & Pebay-Peyroula, E.
The study of membrane-protein /detergent interactions by neutron crystallography.
France.
Timmins, P A, Penel, S, and Pebay-Peyroula, E.
1997.
"The study of membrane-protein /detergent interactions by neutron crystallography."
France.
@misc{etde_593250,
title = {The study of membrane-protein /detergent interactions by neutron crystallography}
author = {Timmins, P A, Penel, S, and Pebay-Peyroula, E}
abstractNote = {Proteins which are found embedded in membranes can usually only be purified and studied from the point of view of structure by dissolving them in detergents. The structure of the resulting mixed protein-detergent complexes are poorly understood. An important method for studying them is through neutron diffraction of the crystalline complexes. This allows us to understand better how the proteins behave in the natural membrane as well as allowing us to visualize and hopefully improve the crystallisation process. Studies on the pore-forming protein porin using data collected on the diffractometer DB21 are described. (author). 4 refs.}
place = {France}
year = {1997}
month = {Apr}
}
title = {The study of membrane-protein /detergent interactions by neutron crystallography}
author = {Timmins, P A, Penel, S, and Pebay-Peyroula, E}
abstractNote = {Proteins which are found embedded in membranes can usually only be purified and studied from the point of view of structure by dissolving them in detergents. The structure of the resulting mixed protein-detergent complexes are poorly understood. An important method for studying them is through neutron diffraction of the crystalline complexes. This allows us to understand better how the proteins behave in the natural membrane as well as allowing us to visualize and hopefully improve the crystallisation process. Studies on the pore-forming protein porin using data collected on the diffractometer DB21 are described. (author). 4 refs.}
place = {France}
year = {1997}
month = {Apr}
}