Detergent micelle structure and micelle-micelle interactions determined by small-angle neutron scattering under solution conditions used for membrane protein crystallization

1994 ◽  
Vol 98 (40) ◽  
pp. 10343-10351 ◽  
Author(s):  
P. Thiyagarajan ◽  
D. M. Tiede
Keyword(s):  
Membrane Protein ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Protein Crystallization ◽  
Detergent Micelle ◽  
Micelle Structure ◽  
Membrane Protein Crystallization

scholarly journals Use of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization

2015 ◽  
Vol 71 (7) ◽  
pp. 838-846 ◽  
Author(s):  
Mohamed Dahani ◽  
Laurie-Anne Barret ◽  
Simon Raynal ◽  
Colette Jungas ◽  
Pétra Pernot ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Membrane Protein ◽  
Small Angle ◽  
Protein Crystallization ◽  
X Ray ◽  
X Ray Scattering ◽  
Membrane Protein Crystallization ◽  
Surfactant Phase ◽  
Ray Scattering

The structural and interactive properties of two novel hemifluorinated surfactants, F2H9-β-M and F4H5-β-M, the syntheses of which were based on the structure and hydrophobicity of the well known dodecyl-β-maltoside (DD-β-M), are described. The shape of their micellar assemblies was characterized by small-angle X-ray scattering and their intermicellar interactions in crystallizing conditions were measured by dynamic light scattering. Such information is essential for surfactant phase-diagram determination and membrane-protein crystallization.

Small-Angle X-ray Scattering Study of Photosystem I−Detergent Complexes:  Implications for Membrane Protein Crystallization

2007 ◽  
Vol 111 (16) ◽  
pp. 4211-4219 ◽  
Author(s):  
Hugh O'Neill ◽  
William T. Heller ◽  
Katherine E. Helton ◽  
Volker S. Urban ◽  
Elias Greenbaum
Keyword(s):  
Membrane Protein ◽  
Photosystem I ◽  
Small Angle ◽  
Protein Crystallization ◽  
X Ray ◽  
X Ray Scattering ◽  
Membrane Protein Crystallization ◽  
Scattering Study ◽  
Ray Scattering

scholarly journals Characterization of lipid matrices for membrane protein crystallization by high-throughput small angle X-ray scattering

Methods ◽  
2011 ◽  
Vol 55 (4) ◽  
pp. 342-349 ◽  
Author(s):  
Jeremiah S. Joseph ◽  
Wei Liu ◽  
Joshua Kunken ◽  
Thomas M. Weiss ◽  
Hiro Tsuruta ◽  
...  
Keyword(s):  
Membrane Protein ◽  
High Throughput ◽  
Small Angle ◽  
Protein Crystallization ◽  
X Ray ◽  
X Ray Scattering ◽  
Membrane Protein Crystallization ◽  
Ray Scattering

Small-Angle Neutron Scattering Study of PEO−PPO−PEO Micelle Structure in the Unimer-to-Micelle Transition Region

Langmuir ◽  
1997 ◽  
Vol 13 (14) ◽  
pp. 3659-3664 ◽  
Author(s):  
Isabella Goldmints ◽  
Friedrich K. von Gottberg ◽  
Kenneth A. Smith ◽  
T. Alan Hatton
Keyword(s):  
Neutron Scattering ◽  
Transition Region ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Micelle Structure ◽  
Scattering Study ◽  
Neutron Scattering Study

scholarly journals Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases

2021 ◽  
Vol 8 ◽  
Author(s):  
Charlotte E. Conn ◽  
Liliana de Campo ◽  
Andrew E. Whitten ◽  
Christopher J. Garvey ◽  
Anwen M. Krause-Heuer ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Neutron Scattering ◽  
Phase Behavior ◽  
Lipid Bilayers ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Protein Structures ◽  
Bicontinuous Cubic ◽  
Contrast Matching ◽  
Detergent Micelles

This perspective describes advances in determining membrane protein structures in lipid bilayers using small-angle neutron scattering (SANS). Differentially labeled detergents with a homogeneous scattering length density facilitate contrast matching of detergent micelles; this has previously been used successfully to obtain the structures of membrane proteins. However, detergent micelles do not mimic the lipid bilayer environment of the cell membrane in vivo. Deuterated vesicles can be used to obtain the radius of gyration of membrane proteins, but protein-protein interference effects within the vesicles severely limits this method such that the protein structure cannot be modeled. We show herein that different membrane protein conformations can be distinguished within the lipid bilayer of the bicontinuous cubic phase using contrast-matching. Time-resolved studies performed using SANS illustrate the complex phase behavior in lyotropic liquid crystalline systems and emphasize the importance of this development. We believe that studying membrane protein structures and phase behavior in contrast-matched lipid bilayers will advance both biological and pharmaceutical applications of membrane-associated proteins, biosensors and food science.

scholarly journals Determining the amphipol distribution within membrane-protein fibre samples using small-angle neutron scattering

2018 ◽  
Vol 74 (12) ◽  
pp. 1192-1199 ◽  
Author(s):  
Wanatchaporn Arunmanee ◽  
Richard K. Heenan ◽  
Jeremy H. Lakey
Keyword(s):  
Membrane Protein ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Oblate Spheroid ◽  
Critical Micellar Concentration ◽  
Polymeric Surfactants ◽  
Contrast Matching ◽  
Outer Membrane Protein F

Detergent micelles can solubilize membrane proteins, but there is always a need for a pool of free detergent at the critical micellar concentration to maintain the micelle–monomer equilibrium. Amphipol polymeric surfactants (APols) have been developed to replace conventional detergents in membrane-protein studies, but the role of free amphipol is unclear. It has previously been shown that the removal of free APol causes monodisperse outer membrane protein F (OmpF) to form long filaments. However, any remaining APol could not be resolved using electron microscopy. Here, small-angle neutron scattering with isotope contrast matching was used to separately determine the distributions of membrane protein and amphipol in a mixed sample. The data showed that after existing free amphipol had been removed from monodisperse complexes, a new equilibrium was established between protein–amphipol filaments and a pool of newly liberated free amphipol. The filaments consisted of OmpF proteins surrounded by a belt of Apol, whilst free oblate spheroid micelles of Apol were also present. No indications of long-range order were observed, suggesting a lack of defined structure in the filaments.

scholarly journals Small-angle Neutron Scattering Study of Micelle Structure and Hydration Behavior of Oleic Acid-based Gemini Surfactant

2019 ◽  
Vol 48 (9) ◽  
pp. 1050-1053 ◽  
Author(s):  
Tadashi Sugahara ◽  
Masaaki Akamatsu ◽  
Hiroki Iwase ◽  
Yuichiro Takamatsu ◽  
Kenichi Sakai ◽  
...  
Keyword(s):  
Oleic Acid ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Gemini Surfactant ◽  
Micelle Structure ◽  
Scattering Study ◽  
Neutron Scattering Study
Sign in / Sign up

Export Citation Format

Share Document