scholarly journals The impact of radical loading and oxidation on the conformation of organic radical polymers by small angle neutron scattering

2018 ◽  
Vol 6 (32) ◽  
pp. 15659-15667 ◽  
Author(s):  
Halie J. Martin ◽  
Barbara K. Hughes ◽  
Wade A. Braunecker ◽  
Thomas Gennett ◽  
Mark D. Dadmun
Keyword(s):  
Molecular Structure ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Organic Radical ◽  
The Impact ◽  
First Time ◽  
Insight Into

SANS provides, for the first time, unique insight into the correlation between organic radical polymer molecular structure and their assembly.

scholarly journals The Structure of Sindbis Virus Produced from Vertebrate and Invertebrate Hosts as Determined by Small-Angle Neutron Scattering

2010 ◽  
Vol 84 (10) ◽  
pp. 5270-5276 ◽  
Author(s):  
Lilin He ◽  
Amanda Piper ◽  
Flora Meilleur ◽  
Dean A. A. Myles ◽  
Raquel Hernandez ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Host Species ◽  
Mammalian Cells ◽  
Small Angle Neutron Scattering ◽  
Sindbis Virus ◽  
Insect Cells ◽  
Lipid Membrane ◽  
Scattering Data ◽  
The Impact

ABSTRACT The complex natural cycle of vectored viruses that transition between host species, such as between insects and mammals, makes understanding the full life cycle of the virus an incredibly complex problem. Sindbis virus, an arbovirus and prototypic alphavirus having an inner protein shell and an outer glycoprotein coat separated by a lipid membrane, is one example of a vectored virus that transitions between vertebrate and insect hosts. While evidence of host-specific differences in Sindbis virus has been observed, no work has been performed to characterize the impact of the host species on the structure of the virus. Here, we report the first study of the structural differences between Sindbis viruses grown in mammalian and insect cells, which were determined by small-angle neutron scattering (SANS), a nondestructive technique that did not decrease the infectivity of the Sindbis virus particles studied. The scattering data and modeling showed that, while the radial position of the lipid bilayer did not change significantly, it was possible to conclude that it did have significantly more cholesterol when the virus was grown in mammalian cells. Additionally, the outer protein coat was found to be more extended in the mammalian Sindbis virus. The SANS data also demonstrated that the RNA and nucleocapsid protein share a closer interaction in the mammalian-cell-grown virus than in the virus from insect cells.

Study on Calibrating Neutron Velocity Selector of Small Angle Neutron Scattering Instrument

2013 ◽  
Vol 433-435 ◽  
pp. 837-843
Author(s):  
Zhou Xiang Yu ◽  
Yun Tao Liu ◽  
He Cheng ◽  
Li Zhang ◽  
Dong Feng Chen
Keyword(s):  
Measurement Error ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Dead Time ◽  
Resolution Rate ◽  
Upper Limits ◽  
Wavelength Resolution ◽  
Total Measurement Time ◽  
First Time

Neutron velocity selector is widely used on neutron scattering instruments as key component. To calibrate it (wavelength and wavelength-resolution-rate measurement), it is necessary to design calibration instrument and develop calibration technique. Based on small angle neutron scattering instrument (SANS) at China Advanced Research Reactor (CARR), instrument structure was designed and instrument parameters were determined. Count loss influence on measurement of wavelength resolution rate (WRR) was studied for the first time. Measurement error of WRR is decided by product of dead time and Gauss peak count rate (GPCR) and increases with increasing GPCR for the same dead time. In order to ensure WRR measurement error less than 0.9%, upper limits of GPCR for detector adjoining chopper and detector far away from chopper are less than 10000[s-1] and 2500[s-1] respectively. According to upper limits of GPCR, floor limit of total measurement time for each spectrum is calculated to be 6.66 minutes.

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

On the design and experimental realization of a multislit-based very small angle neutron scattering instrument at the European Spallation Source

2015 ◽  
Vol 48 (4) ◽  
pp. 1242-1253 ◽  
Author(s):  
Sohrab Abbas ◽  
Sylvain Désert ◽  
Annie Brûlet ◽  
Vincent Thevenot ◽  
Patrice Permingeat ◽  
...  
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Feasibility Studies ◽  
Experimental Realization ◽  
Order Of Magnitude ◽  
Spallation Source ◽  
Length Scaling ◽  
First Time ◽  
Sans Instrument

This article reports the design of a versatile multislit-based very small angle neutron scattering (VSANS) instrument working either as a dedicated instrument or as an add-on for any small-angle neutron scattering machine like the proposed SANS instrument, SKADI, at the future European Spallation Source. The use of multiple slits as a VSANS collimator for the time-of-flight techniques has been validated usingMcStassimulations. Various instrument configurations to achieve different minimum wavevector transfers in scattering experiments are proposed. The flexibility of the multislit VSANS instrument concept is demonstrated by showing the possibility of instrument length scaling for the first time, allowing access to varying minimum wavevector transfers with the same multislit setup. These options can provide smooth access to minimum wavevector transfers lower than ∼4 × 10−5 Å−1and an overlapping of wavevector coverage with normal SANS mode,e.g.with the SKADI wavevector range of 10−3–1.1 Å−1. Such an angularly well defined and intense neutron beam will allow faster SANS studies of objects larger than 1 µm. Calculations have also been carried out for a radial collimator as an alternative to the multislit collimator setup. This extends the SANSQrange by an order of magnitude to 1 × 10−4 Å−1with much simpler alignment. The multislit idea has been realized experimentally by building a prototype at Laboratoire Leon Brillouin, Saclay, with cross-talk-free geometry. Feasibility studies were carried out by making VSANS measurements with single- and multislit collimators, and the results are compared with multiple-pinhole geometry using classical SANS analysis tools.

In situcharacterization of β′′ precipitation in an Al–Mg–Si alloy by anisotropic small-angle neutron scattering on a single crystal

2015 ◽  
Vol 48 (2) ◽  
pp. 455-463 ◽  
Author(s):  
Cynthia Sin Ting Chang ◽  
Frédéric De Geuser ◽  
John Banhart
Keyword(s):  
Neutron Scattering ◽  
Single Crystal ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Scattering Data ◽  
Artificial Ageing ◽  
Number Density ◽  
Transmission Electron ◽  
Repetition Time ◽  
The Impact

A single crystal of an Al–Mg–Si alloy (Mg: 0.43 wt%, Si: 0.47 wt%) was aged at 453 K while small-angle neutron scattering experiments were carried outin situ. The scattering data recorded on a two-dimensional detector show the symmetry typical for needle-shaped β′′ precipitates oriented in the three [100] directions of the aluminium lattice and allow the calculation of the length, diameter and number density of the precipitates assuming cylindrical scattering objects of equal size and composition. The repetition time of the experiments was ∼12 min. The values obtained for the three quantities agree well with values measured by transmission electron microscopy (TEM) on a similar alloy. The impact of one week of natural ageing before artificial ageing on the evolution of the size and number density of precipitates is found to be pronounced, as expected from published TEM data.

Light-induced structural evolution of photoswitchable carbohydrate-based surfactant micelles

2015 ◽  
Vol 51 (25) ◽  
pp. 5509-5512 ◽  
Author(s):  
Rico F. Tabor ◽  
Matthew J. Pottage ◽  
Christopher J. Garvey ◽  
Brendan L. Wilkinson
Keyword(s):  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Structural Changes ◽  
Structural Evolution ◽  
Time Resolved ◽  
Surfactant Micelles ◽  
First Time ◽  
Over Time

We report the light-induced structural evolution of photoswitchable carbohydrate-based surfactant micelles using time-resolved small-angle neutron scattering (TR-SANS), monitoring the structural changes in micellisation in situ over time and demonstrating for the first time the course and implications of this process.

scholarly journals Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase

2020 ◽  
Author(s):  
Daniel T Murray ◽  
Kevin Weiss ◽  
Christopher B Stanley ◽  
Gergely Nagy ◽  
M. Elizabeth Stroupe
Keyword(s):  
Electron Transfer ◽  
Neutron Scattering ◽  
Small Angle ◽  
Small Angle Neutron Scattering ◽  
Single Copy ◽  
Sulfite Reductase ◽  
Solution Structures ◽  
Contrast Matching ◽  
First Time ◽  
Binding Position

Sulfite reductase (SiR), a dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP), reduces sulfur reduction for biomass incorporation. Electron transfer within SiR requires intra- and inter-subunit interactions that are mediated by the relative position of each protein, governed by flexible domain movements. Using small-angle neutron scattering, we report the first solution structures of SiR heterodimers containing a single copy of each subunit. These structures show how the subunits bind and how both subunit binding and oxidation state impact SiRFP's conformation. Neutron contrast matching experiments on selectively deuterated heterodimers allow us to define the contribution of each subunit to the solution scattering. SiRHP binding induces a change in the position of SiRFP's flavodoxin-like domain relative to its ferredoxin-NADP+ reductase domain while compacting SiRHP's N-terminus. Reduction of SiRFP leads to a more open structure relative to its oxidized state, re-positioning SiRFP's N-terminal flavodoxin-like domain towards the SiRHP binding position. These structures show, for the first time, how both SiRHP binding to, and reduction of, SiRFP positions SiRFP for electron transfer between the subunits.

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