scattering experiment
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2022 ◽  
Vol 82 (1) ◽  
Author(s):  
K. D. J. André ◽  
L. Aperio Bella ◽  
N. Armesto ◽  
S. A. Bogacz ◽  
D. Britzger ◽  
...  

AbstractNovel considerations are presented on the physics, apparatus and accelerator designs for a future, luminous, energy frontier electron-hadron (eh) scattering experiment at the LHC in the thirties for which key physics topics and their relation to the hadron-hadron HL-LHC physics programme are discussed. Demands are derived set by these physics topics on the design of the LHeC detector, a corresponding update of which is described. Optimisations on the accelerator design, especially the interaction region (IR), are presented. Initial accelerator considerations indicate that a common IR is possible to be built which alternately could serve eh and hh collisions while other experiments would stay on hh in either condition. A forward-backward symmetrised option of the LHeC detector is sketched which would permit extending the LHeC physics programme to also include aspects of hadron-hadron physics. The vision of a joint eh and hh physics experiment is shown to open new prospects for solving fundamental problems of high energy heavy-ion physics including the partonic structure of nuclei and the emergence of hydrodynamics in quantum field theory while the genuine TeV scale DIS physics is of unprecedented rank.


Author(s):  
Ethan Cline ◽  
Jan Bernauer ◽  
Evangeline J. Downie ◽  
Ronald Gilman

MUSE is a high-precision muon scattering experiment aiming to determine the proton radius. Muon, electron, and pion scattering will be measured at the same time. Two-photon exchange corrections will be determined with data using both beam polarities.


Sensors ◽  
2021 ◽  
Vol 21 (15) ◽  
pp. 5115
Author(s):  
Dan Chicea ◽  
Cristian Leca ◽  
Sorin Olaru ◽  
Liana Maria Chicea

Dynamic Light Scattering is a technique currently used to assess the particle size and size distribution by processing the scattered light intensity. Typically, the particles to be investigated are suspended in a liquid solvent. An analysis of the particular conditions required to perform a light scattering experiment on particles in air is presented in detail, together with a simple experimental setup and the data processing procedure. The results reveal that such an experiment is possible and using the setup and the procedure, both simplified to extreme, enables the design of an advanced sensor for particles and fumes that can output the average size of the particles in air.


2021 ◽  
Vol 43 (2) ◽  
pp. 15-27
Author(s):  
R. Ghazy ◽  
F. Shehata ◽  
F. El-Mekawey ◽  
N. Sayed

2021 ◽  
Vol 56 (5) ◽  
pp. 055003
Author(s):  
L B Calheiro ◽  
W P S Freitas ◽  
C A Martins ◽  
A M B Goncalves

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ashima Sharma ◽  
Tabinda Shakeel ◽  
Mayank Gupta ◽  
Girish H. Rajacharya ◽  
Syed Shams Yazdani

AbstractAcyl-ACP reductase (AAR) is one of the two key cyanobacterial enzymes along with aldehyde deformylating oxygenase (ADO) involved in the synthesis of long-chain alkanes, a drop-in biofuel. The enzyme is prone to aggregation when expressed in Escherichia coli, leading to varying alkane levels. The present work attempts to investigate the crucial structural aspects of AAR protein associated with its stability and folding. Characterization by dynamic light scattering experiment and intact mass spectrometry revealed that recombinantly expressed AAR in E. coli existed in multiple-sized protein particles due to diverse lipidation. Interestingly, while thermal- and urea-based denaturation of AAR showed 2-state unfolding transition in circular dichroism and intrinsic fluorescent spectroscopy, the unfolding process of AAR was a 3-state pathway in GdnHCl solution suggesting that the protein milieu plays a significant role in dictating its folding. Apparent standard free energy $$\left( {\Delta {\text{G}}_{{{\text{NU}}}}^{{{\text{H}}_{2} {\text{O}}}} } \right)$$ Δ G NU H 2 O of ~ 4.5 kcal/mol for the steady-state unfolding of AAR indicated borderline stability of the protein. Based on these evidences, we propose that the marginal stability of AAR are plausible contributing reasons for aggregation propensity and hence the low catalytic activity of the enzyme when expressed in E. coli for biofuel production. Our results show a path for building superior biocatalyst for higher biofuel production.


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