Morphological and Electrical Properties of Stretched Nanoparticle Layers

2015 ◽  
Vol 644 ◽  
pp. 31-34 ◽  
Author(s):  
Ján Ivančo ◽  
Karol Végsö ◽  
Peter Šiffalovič ◽  
Dmytro Kostiuk ◽  
Yurij Halahovets ◽  
...  
Keyword(s):  
Electrical Properties ◽  
Electrical Response ◽  
Interparticle Distance ◽  
Strain Sensors ◽  
Au Nanoparticle ◽  
Gauge Factor ◽  
X Ray ◽  
X Ray Scattering ◽  
Distance Change

To examine perspectives of nanoparticle films in the role of active elements in strain sensors, morphological and electrical properties of self-assembled Au nanoparticle monolayer prepared by modified Langmuir-Schaefer technique onto supporting Mylar foil were studied under elongation. Along the probing of electrical response (characterized by the gauge factor of about 60), the small-angle x-ray scattering (SAXS) characterization assessed an average interparticle distance change, which was shown to vary proportionally to the substrate elongation. The approach allowed to unambiguously address the mechanism of the deformation-resistivity transduction.

scholarly journals Effect of tungsten disulfide nanotubes on crystallization of polylactide under uniaxial deformation and annealing

2021 ◽  
Vol 2 (1) ◽  
Author(s):  
Fausta Loffredo ◽  
Loredana Tammaro ◽  
Tiziana Di Luccio ◽  
Carmela Borriello ◽  
Fulvia Villani ◽  
...  
Keyword(s):  
Biomedical Applications ◽  
Structural Evolution ◽  
Tungsten Disulfide ◽  
Fine Tuning ◽  
Nanocomposite Films ◽  
Uniaxial Deformation ◽  
Scanning Calorimetry ◽  
X Ray ◽  
X Ray Scattering

AbstractTungsten disulfide (WS2) nanotubes (NTs) are examined here as a filler for polylactide (PLA) for their ability to accelerate PLA crystallization and for their promising biocompatibility in relevant to biomedical applications of PLA-WS2 nanocomposites. In this work, we have studied the structural and thermal properties of PLA-WS2 nanocomposite films varying the concentration of WS2 NTs from 0 (neat PLA) to 0.6 wt%. The films were uniaxially drawn at 90 °C and annealed at the same temperature for 3 and 10 min. Using wide angle x-ray scattering, Raman spectroscopy and differential scanning calorimetry, we probed the effects of WS2 NT addition on the structure of the PLA films at various stages of processing (unstretched, stretching, annealing). We found that 0.6 wt% of WS2 induces the same level of crystallinity in as stretched PLA-WS2 as annealing in neat PLA for 10 min. These data provide useful insights into the role of WS2 NTs on the structural evolution of PLA-WS2 composites under uniaxial deformation, and extend their applicability to situations where fine tuning of PLA crystallinity is desirable.

scholarly journals Resonant Inelastic X-ray Scattering on Ferrous and Ferric Bis-imidazole Porphyrin and Cytochromec: Nature and Role of the Axial Methionine–Fe Bond

2014 ◽  
Vol 136 (52) ◽  
pp. 18087-18099 ◽  
Author(s):  
Thomas Kroll ◽  
Ryan G. Hadt ◽  
Samuel A. Wilson ◽  
Marcus Lundberg ◽  
James J. Yan ◽  
...  
Keyword(s):  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Prominent role of oxygen in the multiferroicity ofDyMnO3andTbMnO3: A resonant soft x-ray scattering spectroscopy study

2016 ◽  
Vol 94 (3) ◽  
Author(s):  
S. W. Huang ◽  
J. M. Lee ◽  
Horng-Tay Jeng ◽  
YuCheng Shao ◽  
L. Andrew Wray ◽  
...  
Keyword(s):  
Spectroscopy Study ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals The Role of Intersubunit Interactions for the Stabilization of the T State ofEscherichia coliAspartate Transcarbamoylase

2002 ◽  
Vol 277 (51) ◽  
pp. 49755-49760 ◽  
Author(s):  
Robin S. Chan ◽  
Jessica B. Sakash ◽  
Christine P. Macol ◽  
Jay M. West ◽  
Hiro Tsuruta ◽  
...  
Keyword(s):  
Small Angle ◽  
Structural State ◽  
Aspartate Transcarbamoylase ◽  
Wild Type ◽  
X Ray ◽  
X Ray Scattering ◽  
Intersubunit Interactions ◽  
T State ◽  
Ray Scattering

Homotropic cooperativity inEscherichia coliaspartate transcarbamoylase results from the substrate-induced transition from the T to the R state. These two alternate states are stabilized by a series of interdomain and intersubunit interactions. The salt link between Lys-143 of the regulatory chain and Asp-236 of the catalytic chain is only observed in the T state. When Asp-236 is replaced by alanine the resulting enzyme exhibits full activity, enhanced affinity for aspartate, no cooperativity, and no heterotropic interactions. These characteristics are consistent with an enzyme locked in the functional R state. Using small angle x-ray scattering, the structural consequences of the D236A mutant were characterized. The unliganded D236A holoenzyme appears to be in a new structural state that is neither T, R, nor a mixture of T and R states. The structure of the native D236A holoenzyme is similar to that previously reported for another mutant holoenzyme (E239Q) that also lacks intersubunit interactions. A hybrid version of aspartate transcarbamoylase in which one catalytic subunit was wild-type and the other had the D236A mutation was also investigated. The hybrid holoenzyme, with three of the six possible interactions involving Asp-236, exhibited homotropic cooperativity, and heterotropic interactions consistent with an enzyme with both T and R functional states. Small angle x-ray scattering analysis of the unligated hybrid indicated that the enzyme was in a new structural state more similar to the T than to the R state of the wild-type enzyme. These data suggest that three of the six intersubunit interactions involving D236A are sufficient to stabilize a T-like state of the enzyme and allow for an allosteric transition.

Small-Angle X-Ray Scattering for the Discerning Macromolecular Crystallographer

2014 ◽  
Vol 67 (12) ◽  
pp. 1786 ◽  
Author(s):  
Lachlan W. Casey ◽  
Alan E. Mark ◽  
Bostjan Kobe
Keyword(s):  
Structural Biology ◽  
Small Angle ◽  
Significant Risk ◽  
Macromolecular Crystallography ◽  
Saxs Data ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

The role of small-angle X-ray scattering (SAXS) in structural biology is now well established, and its usefulness in combination with macromolecular crystallography is clear. However, the highly averaged SAXS data present a significant risk of over-interpretation to the unwary practitioner, and it can be challenging to frame SAXS results in a manner that maximises the reliability of the conclusions drawn. In this review, a series of recent examples are used to illustrate both the challenges for interpretation and approaches through which these can be overcome.

Role of boron on grain sizes and magnetic correlation lengths in recording media as determined by soft x-ray scattering

2002 ◽  
Vol 80 (7) ◽  
pp. 1234-1236 ◽  
Author(s):  
Olav Hellwig ◽  
D. T. Margulies ◽  
B. Lengsfield ◽  
Eric E. Fullerton ◽  
J. B. Kortright
Keyword(s):  
Recording Media ◽  
Correlation Lengths ◽  
X Ray ◽  
Magnetic Correlation ◽  
Grain Sizes ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals The role of the ionic liquid C6C1ImTFSI in the sol–gel synthesis of silica studied using in situ SAXS and Raman spectroscopy

2015 ◽  
Vol 17 (15) ◽  
pp. 9841-9848 ◽  
Author(s):  
Moheb Nayeri ◽  
Kim Nygård ◽  
Maths Karlsson ◽  
Manuel Maréchal ◽  
Manfred Burghammer ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Ionic Liquid ◽  
Sol Gel ◽  
Chemical Changes ◽  
X Ray ◽  
X Ray Scattering ◽  
Sol Gel Synthesis ◽  
Ray Scattering

Structural and chemical changes during the sol–gel synthesis of silica using an ionic liquid are investigatedin situand simultaneously by X-ray scattering and μ-Raman spectroscopy.

scholarly journals Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states

2013 ◽  
Vol 69 (10) ◽  
pp. 2050-2060 ◽  
Author(s):  
Bodo Sander ◽  
Giancarlo Tria ◽  
Alexander V. Shkumatov ◽  
Eun-Young Kim ◽  
J. Günter Grossmann ◽  
...  
Keyword(s):  
Conformational Dynamics ◽  
Cd Spectroscopy ◽  
X Ray ◽  
Force Microscopy ◽  
X Ray Scattering ◽  
Atomic Force ◽  
Extended States ◽  
High Degree

Gephyrin is a trimeric protein involved in the final steps of molybdenum-cofactor (Moco) biosynthesis and in the clustering of inhibitory glycine and GABAAreceptors at postsynaptic specializations. Each protomer consists of stably folded domains (referred to as the G and E domains) located at either terminus and connected by a proteolytically sensitive linker of ∼150 residues. Both terminal domains can oligomerize in their isolated forms; however, in the context of the full-length protein only the G-domain trimer is permanently present, whereas E-domain dimerization is prevented. Atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS) reveal a high degree of flexibility in the structure of gephyrin. The results imply an equilibrium between compact and extended conformational states in solution, with a preference for compact states. CD spectroscopy suggests that a partial compaction is achieved by interactions of the linker with the G and E domains. Taken together, the data provide a rationale for the role of the linker in the overall structure and the conformational dynamics of gephyrin.

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