scholarly journals Critical Role of Micelles in Pancreatic Lipase Activation Revealed by Small Angle Neutron Scattering

2000 ◽  
Vol 275 (6) ◽  
pp. 4220-4224 ◽  
Author(s):  
David Pignol ◽  
Laurence Ayvazian ◽  
Brigitte Kerfelec ◽  
Peter Timmins ◽  
Isabelle Crenon ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Pancreatic Lipase ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Critical Role

scholarly journals Small-Angle Neutron Scattering of Ionic Perfluoropolyether Micellar Solutions:  Role of Counterions and Temperature

2005 ◽  
Vol 109 (18) ◽  
pp. 8592-8598 ◽  
Author(s):  
C. M. C. Gambi ◽  
R. Giordano ◽  
A. Chittofrati ◽  
R. Pieri ◽  
P. Baglioni ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Micellar Solutions

New insight into the structure of RNA in red clover necrotic mosaic virus and the role of divalent cations revealed by small-angle neutron scattering

2013 ◽  
Vol 158 (8) ◽  
pp. 1661-1669 ◽  
Author(s):  
Stanton L. Martin ◽  
Lilin He ◽  
Flora Meilleur ◽  
Richard H. Guenther ◽  
Tim L. Sit ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Mosaic Virus ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Divalent Cations ◽  
Red Clover ◽  
Insight Into

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.

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