Nanostructure of Fullerene-Bearing Artificial Lipid Monolayer on Water Surface by in Situ X-ray Reflectometry

Langmuir ◽  
2002 ◽  
Vol 18 (25) ◽  
pp. 10042-10045 ◽  
Author(s):  
Emiko Mouri ◽  
Takashi Nakanishi ◽  
Naotoshi Nakashima ◽  
Hideki Matsuoka
Keyword(s):  
Langmuir ◽  
2002 ◽  
Vol 18 (10) ◽  
pp. 3875-3879 ◽  
Author(s):  
Keitaro Kago ◽  
Takahiro Seki ◽  
Randolf R. Schücke ◽  
Emiko Mouri ◽  
Hideki Matsuoka ◽  
...  

1997 ◽  
Vol 30 (21) ◽  
pp. 6633-6639 ◽  
Author(s):  
Hubert Baltes ◽  
Michael Schwendler ◽  
Christiane A. Helm ◽  
Robert Heger ◽  
Werner A. Goedel

2021 ◽  
Vol 5 (2) ◽  
pp. 31
Author(s):  
Yohko F. Yano ◽  
Toshiaki Ina ◽  
Tomoya Uruga

Biological membrane is composed of lipid molecules, because of its fluidity, it is possible to carry out physiological functions. Therefore, it is important to study the hydrodynamic properties of membranes toward understanding its function. Here, we observed the dynamical behavior of a lipid monolayer on the water surface under Marangoni flow. By using X-ray reflectometry, we obtained the tilt angle of the hydrocarbon chains of the lipid at different surface pressures. Comparing them with the dynamical surface pressure under Marangoni flow, it was found that the lipid molecules in rotational rather than translational motion. At low surface pressure, the molecular tilt angle is reduced by 20 degrees, even though the molecular area is reduced by at most 10%.


Author(s):  
R. E. Herfert

Studies of the nature of a surface, either metallic or nonmetallic, in the past, have been limited to the instrumentation available for these measurements. In the past, optical microscopy, replica transmission electron microscopy, electron or X-ray diffraction and optical or X-ray spectroscopy have provided the means of surface characterization. Actually, some of these techniques are not purely surface; the depth of penetration may be a few thousands of an inch. Within the last five years, instrumentation has been made available which now makes it practical for use to study the outer few 100A of layers and characterize it completely from a chemical, physical, and crystallographic standpoint. The scanning electron microscope (SEM) provides a means of viewing the surface of a material in situ to magnifications as high as 250,000X.


Author(s):  
Peter D. Moisiuk ◽  
Daniel R. Beniac ◽  
Ross A. Ridsdale ◽  
Martin Young ◽  
Bhushan Nagar ◽  
...  

Venom from the rattlesnake Crotalus atrox contains a mixture of enzymes that induce a localized effect leading to hemorrhaging, necrosis and edema. As a member of the crotalid family of snake venoms, Crotalus atrox venom contains a C-type lectin that will agglutinate blood cells in a Ca2+-dependent fashion. The lectin is a hydrophilic protein, consisting of two covalently linked, 135 amino acid residues, identical subunits that are rich in aspartic acid, glutamic acid and lysine. Sequence homology with known carbohydrate recognition domains (CRDs) indicates that rattlesnake venom lectin (RSLV) contains a CRD motif that is not linked to accessory domains. Preliminary X-ray diffraction and sedimentation analysis has indicated that lectin from Crotalus atrox forms decamers composed of two five-fold symmetric pentamers. Single particles of RSVL imaged at – 171°C displayed two distinct orientations on the specimen support (Figure a) following incubation in a crystallization Teflon well, coated with a lipid monolayer consisting of phosphatidylcholine and monosialoganglioside. When lying in an end-on orientation, the lectin exhibited a “pentagonal ring” with an outer diameter of 6.7 nm and an inner hollow core of 1.7 nm. A side orientation was also seen, whereby a thickness of 5.8 nm was measured for the lectin. Image processing of 2280 single particles placed in 100 classes (Figure b) led to 3D reconstructions of RSVL (Figure c). Density limited 3D reconstructions showed the lectin to be made of two five-fold symmetrical rings covalently linked between the five subunits that constitute each ring of this homodimer. These results are consistent with sedimentation and preliminary X-ray diffraction analysis on the shape of RSVL and provide the framework for structural verification by 2D electron crystallography.


2005 ◽  
Vol 72 ◽  
pp. 177-188 ◽  
Author(s):  
Félix M. Goñi ◽  
F-Xabier Contreras ◽  
L-Ruth Montes ◽  
Jesús Sot ◽  
Alicia Alonso

In the past decade, the long-neglected ceramides (N-acylsphingosines) have become one of the most attractive lipid molecules in molecular cell biology, because of their involvement in essential structures (stratum corneum) and processes (cell signalling). Most natural ceramides have a long (16-24 C atoms) N-acyl chain, but short N-acyl chain ceramides (two to six C atoms) also exist in Nature, apart from being extensively used in experimentation, because they can be dispersed easily in water. Long-chain ceramides are among the most hydrophobic molecules in Nature, they are totally insoluble in water and they hardly mix with phospholipids in membranes, giving rise to ceramide-enriched domains. In situ enzymic generation, or external addition, of long-chain ceramides in membranes has at least three important effects: (i) the lipid monolayer tendency to adopt a negative curvature, e.g. through a transition to an inverted hexagonal structure, is increased, (ii) bilayer permeability to aqueous solutes is notoriously enhanced, and (iii) transbilayer (flip-flop) lipid motion is promoted. Short-chain ceramides mix much better with phospholipids, promote a positive curvature in lipid monolayers, and their capacities to increase bilayer permeability or transbilayer motion are very low or non-existent.


1997 ◽  
Vol 7 (C2) ◽  
pp. C2-619-C2-620 ◽  
Author(s):  
M. Giorgett ◽  
I. Ascone ◽  
M. Berrettoni ◽  
S. Zamponi ◽  
R. Marassi

2019 ◽  
Author(s):  
Christian Prehal ◽  
Aleksej Samojlov ◽  
Manfred Nachtnebel ◽  
Manfred Kriechbaum ◽  
Heinz Amenitsch ◽  
...  

<b>Here we use in situ small and wide angle X-ray scattering to elucidate unexpected mechanistic insights of the O2 reduction mechanism in Li-O2 batteries.<br></b>


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