singular interactions
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Symmetry ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 978
Author(s):  
Nathan M. Myers ◽  
Jacob McCready ◽  
Sebastian Deffner

By harnessing quantum phenomena, quantum devices have the potential to outperform their classical counterparts. Here, we examine using wave function symmetry as a resource to enhance the performance of a quantum Otto engine. Previous work has shown that a bosonic working medium can yield better performance than a fermionic medium. We expand upon this work by incorporating a singular interaction that allows the effective symmetry to be tuned between the bosonic and fermionic limits. In this framework, the particles can be treated as anyons subject to Haldane’s generalized exclusion statistics. Solving the dynamics analytically using the framework of “statistical anyons”, we explore the interplay between interparticle interactions and wave function symmetry on engine performance.


2020 ◽  
Vol 279 (8) ◽  
pp. 108700
Author(s):  
Jussi Behrndt ◽  
Markus Holzmann ◽  
Thomas Ourmières-Bonafos ◽  
Konstantin Pankrashkin

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Julien Pernier ◽  
Remy Kusters ◽  
Hugo Bousquet ◽  
Thibaut Lagny ◽  
Antoine Morchain ◽  
...  

AbstractThe regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end.


2018 ◽  
Author(s):  
Julien Pernier ◽  
Remy Kusters ◽  
Hugo Bousquet ◽  
Thibaut Lagny ◽  
Antoine Morchain ◽  
...  

AbstractThe regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. We investigate the contribution of myosin1b to actin dynamics using sliding motility assays. We observe that sliding on myosin1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as a new type of depolymerase and points to its singular interactions with the actin barbed end.


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