scholarly journals Flow through Constriction in an Open Channel

1984 ◽  
Vol 28 ◽  
pp. 161-166
Keyword(s):  
2016 ◽  
Vol 15 (0) ◽  
pp. 22
Author(s):  
Rupak Saha ◽  
Sanchayan Mukherjee ◽  
Ajay Kumar Das ◽  
Kanhu Keshab Jena ◽  
Manajit Mandal ◽  
...  
Keyword(s):  

2020 ◽  
Vol 32 (4) ◽  
pp. 795-799
Author(s):  
Wei-jie Wang ◽  
Xiao-yu Cui ◽  
Fei Dong ◽  
Wen-qi Peng ◽  
Zhen Han ◽  
...  

1989 ◽  
Vol 16 (5) ◽  
pp. 774-777 ◽  
Author(s):  
N. Rajaratnam ◽  
C. Katopodis ◽  
A. Mainali

This technical note presents a method of analyzing the flow in pool-orifice fishways by dividing it into vertical slot and submerged orifice flow regimes. For a pool-orifice-weir fishway, with flow through the orifice as well as over the weir, a method has been suggested for predicting the total flow rate in the fishway. Experimental observations are presented in support of these methods. Key words: open-channel flow, hydraulics, fishways, turbulent flow.


2002 ◽  
Vol 119 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Brad S. Rothberg ◽  
Ki Soon Shin ◽  
Prashant S. Phale ◽  
Gary Yellen

Hyperpolarization-activated cation (HCN) channels regulate pacemaking activity in cardiac cells and neurons. Our previous work using the specific HCN channel blocker ZD7288 provided evidence for an intracellular activation gate for these channels because it appears that ZD7288, applied from the intracellular side, can enter and leave HCN channels only at voltages where the activation gate is opened (Shin, K.S., B.S. Rothberg, and G. Yellen. 2001. J. Gen. Physiol. 117:91–101). However, the ZD7288 molecule is larger than the Na+ or K+ ions that flow through the open channel. In the present study, we sought to resolve whether the voltage gate at the intracellular entrance to the pore for ZD7288 also can be a gate for permeant ions in HCN channels. Single residues in the putative pore-lining S6 region of an HCN channel (cloned from sea urchin; spHCN) were substituted with cysteines, and the mutants were probed with Cd2+ applied to the intracellular side of the channel. One mutant, T464C, displayed rapid irreversible block when Cd2+ was applied to opened channels, with an apparent blocking rate of ∼3 × 105 M−1s−1. The blocking rate was decreased for channels held at more depolarized voltages that close the channels, which is consistent with the Cd2+ access to this residue being gated from the intracellular side of the channel. 464C channels could be recovered from Cd2+ inhibition in the presence of a dithiol applied to the intracellular side. The rate of this recovery also was reduced when channels were held at depolarized voltages. Finally, Cd2+ could be trapped inside channels that were composed of WT/464C tandem-linked subunits, which could otherwise recover spontaneously from Cd2+ inhibition. Thus, Cd2+ escape is also gated at the intracellular side of the channel. Together, these results are consistent with a voltage-controlled structure at the intracellular side of the spHCN channel that can gate the flow of cations through the pore.


1984 ◽  
Author(s):  
F. SAHELI ◽  
B. DUNN ◽  
K. MARRS ◽  
A. KUMAR ◽  
K. PEERY

2005 ◽  
pp. 395-428 ◽  
Author(s):  
C.A.M.E. Wilson ◽  
T. Stoesser ◽  
P.D. Bates

2014 ◽  
Vol 52 (5) ◽  
pp. 630-643 ◽  
Author(s):  
Jonathan M. Tsikata ◽  
Mark F. Tachie ◽  
Christos Katopodis

Sign in / Sign up

Export Citation Format

Share Document