Contrast-Matching Small-Angle Neutron Scattering to Monitor the Accessibility of Solvents to the Porosity of Coked FCC Catalysts

2002 ◽  
Vol 41 (25) ◽  
pp. 6566-6571 ◽  
Author(s):  
Miguel Castro Diaz ◽  
Peter J. Hall ◽  
Colin E. Snape ◽  
Steven D. Brown ◽  
Ron Hughes
1996 ◽  
Vol 92 (14) ◽  
pp. 2607-2610 ◽  
Author(s):  
Peter J. Hall ◽  
Wilson Ruiz Machado ◽  
David Gascon Galan ◽  
Elizabeth Barrientos Barria ◽  
David C. Sherrington

Carbon ◽  
2012 ◽  
Vol 50 (14) ◽  
pp. 5062-5075 ◽  
Author(s):  
Z. Mileeva ◽  
D.K. Ross ◽  
D. Wilkinson ◽  
S.M. King ◽  
T.A. Ryan ◽  
...  

2018 ◽  
Vol 188 ◽  
pp. 156-164 ◽  
Author(s):  
Jitendra Bahadur ◽  
Leslie F. Ruppert ◽  
Vitaliy Pipich ◽  
Richard Sakurovs ◽  
Yuri B. Melnichenko

1988 ◽  
Vol 132 ◽  
Author(s):  
J. A. Eastman ◽  
J. E. Epperson ◽  
H. Hahn ◽  
T. E. Klippert ◽  
A. Narayanasamy ◽  
...  

ABSTRACTNanophase titanium, prepared by the gas-condensation method both as aggregated powder and in lightly compacted discs, has been studied by conventional small angle neutron scattering, and by use of contrast variation methods. The contrast has been changed (a), isotopically, by means of deuterated/protonated solvents distilled into the specimen and (b) by progressive incremental oxidation of the Ti particles using fixed doses of low-pressure oxygen. It was shown that some evolution of the small angle pattern for lightly compacted nanophase Ti occurred over a period of several months at 300 K. Contrast matching by external solvent works well and has allowed the scattering lengths of oxidized and unoxidized specimens to be followed. The results imply that the scattering from metal and oxide can be separated under suitable conditions. The partial oxidation experiments indicate that there is both a fast and slow oxidation at 300 K. Also, during slow oxidation, high scattering length density scattering centers were formed whose number increased, but whose size remained the same at about 2 nm; these centers are tentatively assumed to be TiO2.


1988 ◽  
Vol 21 (6) ◽  
pp. 1802-1806 ◽  
Author(s):  
Yushu Matsushita ◽  
Yasushi Nakao ◽  
Ryuichi Saguchi ◽  
Katsuaki Mori ◽  
Haruhisa Choshi ◽  
...  

Author(s):  
Nobuhiro Sato ◽  
Rina Yogo ◽  
Saeko Yanaka ◽  
Anne Martel ◽  
Lionel Porcar ◽  
...  

Abstract Small-angle neutron scattering (SANS) and small- angle X-ray scattering (SAXS) are powerful techniques for the structural characterization of biomolecular complexes. In particular, SANS enables a selective observation of specific components in complexes by selective deuteration with contrast-matching techniques. In most cases, however, biomolecular interaction systems with heterogeneous oligomers often contain unfavorable aggregates and unbound species, hampering data interpretation. To overcome these problems, SAXS has been recently combined with size exclusion chromatography (SEC), which enables the isolation of the target complex in a multi-component system. By contrast, SEC–SANS is only at a preliminary stage. Hence, we herein perform a feasibility study of this method based on our newly developed inverse contrast-matching (iCM) SANS technique using antibody interactions as model systems. Immunoglobulin G (IgG) or its Fc fragment was mixed with 75% deuterated Fc-binding proteins, i.e. a mutated form of IgG-degrading enzyme of Streptococcus pyogenes and a soluble form of Fcγ receptor IIIb, and subjected to SEC–SANS as well as SEC–SAXS as reference. We successfully observe SANS from the non-deuterated IgG or Fc formed in complex with these binding partners, which were unobservable in terms of SANS in D2O, hence demonstrating the potential utility of the SEC–iCM–SANS approach.


2021 ◽  
Vol 8 ◽  
Author(s):  
Charlotte E. Conn ◽  
Liliana de Campo ◽  
Andrew E. Whitten ◽  
Christopher J. Garvey ◽  
Anwen M. Krause-Heuer ◽  
...  

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.


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