scholarly journals Charge dynamics in half-filled Hubbard chains with finite on-site interaction

2012 ◽  
Vol 85 (16) ◽  
Author(s):  
R. G. Pereira ◽  
K. Penc ◽  
S. R. White ◽  
P. D. Sacramento ◽  
J. M. P. Carmelo
Keyword(s):  
Author(s):  
Dengyang Guo ◽  
Zahra Garmaroudi ◽  
Samuel Stranks ◽  
Tom Savenije

2021 ◽  
Vol 104 (2) ◽  
Author(s):  
M. Nakajima ◽  
K. Yanase ◽  
M. Kawai ◽  
D. Asami ◽  
T. Ishikawa ◽  
...  

Author(s):  
Ayushi Singh ◽  
Ashish Kumar Singh ◽  
Jian-Qiang Liu ◽  
Abhinav Kumar

Metal-organic frameworks (MOFs) or coordination polymers (CPs) are regarded as new variety of materials that find potential applications in plethora of areas such as gas/small molecule absorption/separation, gas storage, membranes...


RSC Advances ◽  
2021 ◽  
Vol 11 (20) ◽  
pp. 12288-12305
Author(s):  
Yi-An Chen ◽  
Yu-Ting Wang ◽  
Hyun Sik Moon ◽  
Kijung Yong ◽  
Yung-Jung Hsu

This review gives a comprehensive retrospection on the preparation and photocatalytic applications of yolk–shell nanostructures with additional focus on the realization of interfacial charge dynamics.


1992 ◽  
Vol 46 (6) ◽  
pp. 3410-3419 ◽  
Author(s):  
J. Deisz ◽  
K.-H. Luk ◽  
M. Jarrell ◽  
D. L. Cox
Keyword(s):  

2006 ◽  
Vol 128 (6) ◽  
pp. 745-753 ◽  
Author(s):  
Kevin Dougherty ◽  
Manuel Covarrubias

Dipeptidyl aminopeptidase–like proteins (DPLPs) interact with Kv4 channels and thereby induce a profound remodeling of activation and inactivation gating. DPLPs are constitutive components of the neuronal Kv4 channel complex, and recent observations have suggested the critical functional role of the single transmembrane segment of these proteins (Zagha, E., A. Ozaita, S.Y. Chang, M.S. Nadal, U. Lin, M.J. Saganich, T. McCormack, K.O. Akinsanya, S.Y. Qi, and B. Rudy. 2005. J. Biol. Chem. 280:18853–18861). However, the underlying mechanism of action is unknown. We hypothesized that a unique interaction between the Kv4.2 channel and a DPLP found in brain (DPPX-S) may remodel the channel's voltage-sensing domain. To test this hypothesis, we implemented a robust experimental system to measure Kv4.2 gating currents and study gating charge dynamics in the absence and presence of DPPX-S. The results demonstrated that coexpression of Kv4.2 and DPPX-S causes a −26 mV parallel shift in the gating charge-voltage (Q-V) relationship. This shift is associated with faster outward movements of the gating charge over a broad range of relevant membrane potentials and accelerated gating charge return upon repolarization. In sharp contrast, DPPX-S had no effect on gating charge movements of the Shaker B Kv channel. We propose that DPPX-S destabilizes resting and intermediate states in the voltage-dependent activation pathway, which promotes the outward gating charge movement. The remodeling of gating charge dynamics may involve specific protein–protein interactions of the DPPX-S's transmembrane segment with the voltage-sensing and pore domains of the Kv4.2 channel. This mechanism may determine the characteristic fast operation of neuronal Kv4 channels in the subthreshold range of membrane potentials.


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