Investigation of Pore-Blocking Mechanism in Gravel Packs in the Management and Control of Fines Migration

Author(s):  
Yann Bigno ◽  
M.B. Oyeneyin ◽  
J.M. Peden
2020 ◽  
Vol 184 ◽  
pp. 106512 ◽  
Author(s):  
Marzieh Ghadimi ◽  
Mojtaba Ghaedi ◽  
Mohammad R. Malayeri ◽  
Mohammad J. Amani

2017 ◽  
Vol 800 ◽  
pp. 40-47 ◽  
Author(s):  
Leticia G. Marmolejo-Murillo ◽  
Iván A. Aréchiga-Figueroa ◽  
Eloy G. Moreno-Galindo ◽  
Ricardo A. Navarro-Polanco ◽  
Aldo A. Rodríguez-Menchaca ◽  
...  

2017 ◽  
Vol 149 (4) ◽  
pp. 511-522 ◽  
Author(s):  
Daniel L. Turman ◽  
Randy B. Stockbridge

The Fluc family of proteins comprises small, electrodiffusive fluoride channels, which prevent accumulation of toxic F− ions in microorganisms. Recent crystal structures have confirmed their unusual architecture, in which a pair of antiparallel subunits convenes to form a dimer with a twofold symmetry axis parallel to the plane of the membrane. These structures have also revealed the interactions between Fluc channels and several different fibronectin domain monobodies that inhibit Fluc-mediated F− currents; in all structures, each channel binds to two monobodies symmetrically, one on either side of the membrane. However, these structures do not reveal the mechanism of monobody inhibition. Moreover, the results appear to diverge from a recent electrophysiological study indicating that monobody binding is negatively cooperative; that is, a bound monobody on one side of a Fluc channel decreases the affinity of an oppositely bound monobody by ∼10-fold. In this study, we reconcile these observations by probing the mechanism of monobody binding and its negative cooperativity using electrophysiological experiments in planar lipid bilayers. Our results indicate that monobody inhibition occurs via a pore-blocking mechanism and that negative cooperativity arises from electrostatic repulsion between the oppositely bound monobodies. A single glutamate residue, on a loop of the monobody that extends into the channel interior, is responsible for negatively cooperative binding. This glutamate side chain also confers voltage dependence and sensitivity to the concentration of trans-F− ion to monobody binding. Neutralization by mutation to glutamine abolishes these electrostatic effects. Monobodies that are amenable to cocrystallization with Fluc channels lack an analogous negatively charged side chain and bind independently to opposite sides of the channel. Thus, this work reveals the source of voltage dependence and negative cooperativity of monobody binding to Fluc channels along with the pore-blocking mechanism.


Channels ◽  
2009 ◽  
Vol 3 (6) ◽  
pp. 448-461 ◽  
Author(s):  
Henry H. Jerng ◽  
Kevin Dougherty ◽  
Manuel Covarrubias ◽  
Paul J. Pfaffinger

2016 ◽  
Vol 51 (12) ◽  
pp. 2047-2061 ◽  
Author(s):  
Mutiu Kolade Amosa ◽  
Mohammed Saedi Jami ◽  
Ma’an Fahmi R. Alkhatib ◽  
Thokozani Majozi

2007 ◽  
Author(s):  
Nelson Chavez ◽  
Oscar Colmenares ◽  
Alejandro Andres Pena ◽  
Argenis Fuenmayor ◽  
Virgilio de Sousa ◽  
...  

Author(s):  
R. R. Dils ◽  
P. S. Follansbee

Electric fields have been applied across oxides growing on a high temperature alloy and control of the oxidation of the material has been demonstrated. At present, three-fold increases in the oxidation rate have been measured in accelerating fields and the oxidation process has been completely stopped in a retarding field.The experiments have been conducted with an iron-base alloy, Pe 25Cr 5A1 0.1Y, although, in principle, any alloy capable of forming an adherent aluminum oxide layer during oxidation can be used. A specimen is polished and oxidized to produce a thin, uniform insulating layer on one surface. Three platinum electrodes are sputtered on the oxide surface and the specimen is reoxidized.


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