Examining Membrane Proteins by Neutron Scattering

2020 ◽  
pp. 147-175
Author(s):  
Christine Ebel ◽  
Cécile Breyton ◽  
Anne Martel
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering

Small angle neutron scattering for the study of solubilised membrane proteins

2013 ◽  
Vol 36 (7) ◽  
Author(s):  
Cécile Breyton ◽  
Frank Gabel ◽  
Mathilde Lethier ◽  
Ali Flayhan ◽  
Grégory Durand ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering

scholarly journals Diisobutylene Maleic Acid Copolymer (DIBMA) Lipid Particle: A “Stealth” Membrane Mimetic for Neutron Scattering

2020 ◽  
Author(s):  
Rong Guo ◽  
Jacob Sumner ◽  
Shuo Qian
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering ◽  
Maleic Acid ◽  
Contrast Variation ◽  
Acid Copolymer ◽  
Membrane Mimetic ◽  
Lipid Particles ◽  
Lipid Particle ◽  
Contrast Matching ◽  
Maleic Acid Copolymer

Diisobutylene maleic acid (DIBMA) has been shown to solubilize and purify membrane proteins from a native lipid bilayer into nanodiscs without the need for a detergent. To explore DIBMA lipid particles as a suitable membrane mimetic system for neutron scattering studies of membrane proteins, we measured and determined the contrast matching point of DIBMA to be ~12% (v/v) D2O—similar to that of most protiated lipid molecules, but distinct from that of regular protiated proteins, providing a natural contrast for separating neutron scattering signals. Using SANS contrast variation, we demonstrated that the scattering from the whole lipid particle can be annihilated. Further, the lipid part of the particle shows a well-defined discoidal shape with DIBMA contrast matched. These results demonstrate that the DIBMA lipid particle is an outstanding “stealth” membrane mimetic for membrane proteins.<br>

Biological small-angle neutron scattering: recent results and development

2018 ◽  
Vol 74 (8) ◽  
pp. 715-726 ◽  
Author(s):  
Emilie Mahieu ◽  
Frank Gabel
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering ◽  
Structural Biology ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Protein Complexes ◽  
Limited Range ◽  
Density Variation ◽  
Deuterium Labelling ◽  
Recent Developments

Small-angle neutron scattering (SANS) has increasingly been used by the structural biology community in recent years to obtain low-resolution information on solubilized biomacromolecular complexes in solution. In combination with deuterium labelling and solvent-contrast variation (H2O/D2O exchange), SANS provides unique information on individual components in large heterogeneous complexes that is perfectly complementary to the structural restraints provided by crystallography, nuclear magnetic resonance and electron microscopy. Typical systems studied include multi-protein or protein–DNA/RNA complexes and solubilized membrane proteins. The internal features of these systems are less accessible to the more broadly used small-angle X-ray scattering (SAXS) technique owing to a limited range of intra-complex and solvent electron-density variation. Here, the progress and developments of biological applications of SANS in the past decade are reviewed. The review covers scientific results from selected biological systems, including protein–protein complexes, protein–RNA/DNA complexes and membrane proteins. Moreover, an overview of recent developments in instruments, sample environment, deuterium labelling and software is presented. Finally, the perspectives for biological SANS in the context of integrated structural biology approaches are discussed.

X-ray and Neutron Scattering Study of Membrane Proteins in Solution

1983 ◽  
pp. 283-298 ◽  
Author(s):  
V. Luzzati ◽  
A. Tardieu ◽  
C. Sardet ◽  
M. le Maire ◽  
H. B. Osborne ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering ◽  
X Ray ◽  
Scattering Study ◽  
Neutron Scattering Study

scholarly journals Diisobutylene Maleic Acid Copolymer (DIBMA) Lipid Particle: A “Stealth” Membrane Mimetic for Neutron Scattering

2020 ◽  
Author(s):  
Rong Guo ◽  
Jacob Sumner ◽  
Shuo Qian
Keyword(s):  
Membrane Proteins ◽  
Neutron Scattering ◽  
Maleic Acid ◽  
Contrast Variation ◽  
Acid Copolymer ◽  
Membrane Mimetic ◽  
Lipid Particles ◽  
Lipid Particle ◽  
Contrast Matching ◽  
Maleic Acid Copolymer

Diisobutylene maleic acid (DIBMA) has been shown to solubilize and purify membrane proteins from a native lipid bilayer into nanodiscs without the need for a detergent. To explore DIBMA lipid particles as a suitable membrane mimetic system for neutron scattering studies of membrane proteins, we measured and determined the contrast matching point of DIBMA to be ~12% (v/v) D2O—similar to that of most protiated lipid molecules, but distinct from that of regular protiated proteins, providing a natural contrast for separating neutron scattering signals. Using SANS contrast variation, we demonstrated that the scattering from the whole lipid particle can be annihilated. Further, the lipid part of the particle shows a well-defined discoidal shape with DIBMA contrast matched. These results demonstrate that the DIBMA lipid particle is an outstanding “stealth” membrane mimetic for membrane proteins.<br>

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