MCU Regulation in Lipid Bilayer and Electrophysiological Recording

2019 ◽  
pp. 59-63
Author(s):  
Vanessa Checchetto ◽  
Ildikò Szabò
Keyword(s):  
Lipid Bilayer ◽  
Electrophysiological Recording

Fate of sperm membrane in fertilized ova

1993 ◽  
Vol 51 ◽  
pp. 40-41
Author(s):  
Frank J. Longo
Keyword(s):  
Electron Microscopy ◽  
Electrical Activity ◽  
Sea Urchins ◽  
Morphological Changes ◽  
Integrated System ◽  
Electrophysiological Recording ◽  
Experimental Conditions ◽  
The Status ◽  
Sperm Membrane ◽  
Temporal And Spatial

Measurement of the egg's electrical activity, the fertilization potential or the activation current (in voltage clamped eggs), provides a means of detecting the earliest perceivable response of the egg to the fertilizing sperm. By using the electrical physiological record as a “real time” indicator of the instant of electrical continuity between the gametes, eggs can be inseminated with sperm at lower, more physiological densities, thereby assuring that only one sperm interacts with the egg. Integrating techniques of intracellular electrophysiological recording, video-imaging, and electron microscopy, we are able to identify the fertilizing sperm precisely and correlate the status of gamete organelles with the first indication (fertilization potential/activation current) of the egg's response to the attached sperm. Hence, this integrated system provides improved temporal and spatial resolution of morphological changes at the site of gamete interaction, under a variety of experimental conditions. Using these integrated techniques, we have investigated when sperm-egg plasma membrane fusion occurs in sea urchins with respect to the onset of the egg's change in electrical activity.

Nano-pore Lipid Bilayer Formed by Self-spreading Method

2019 ◽  
Vol 139 (10) ◽  
pp. 1146-1152
Author(s):  
Zugui Peng ◽  
Kenta Shimba ◽  
Yoshitaka Miyamoto ◽  
Tohru Yagi
Keyword(s):  
Lipid Bilayer

Spotting Differences in Molecular Dynamic Simulations of Influenza A M2 Protein-Ligand Complexes by Varying M2 construct, Lipid Bilayer and Force Field

2019 ◽  
Author(s):  
Dimitrios Kolokouris ◽  
Iris Kalenderoglou ◽  
Panagiotis Lagarias ◽  
Antonios Kolocouris
Keyword(s):  
Molecular Dynamic ◽  
Lipid Bilayer ◽  
Influenza A ◽  
Md Simulations ◽  
Membrane Curvature ◽  
Buffer Size ◽  
M2 Protein ◽  
Dynamic Simulations ◽  
Amphipathic Helices ◽  
Drug Protein Binding

<p>We studied by molecular dynamic (MD) simulations systems including the inward<sub>closed</sub> state of influenza A M2 protein in complex with aminoadamantane drugs in membrane bilayers. We varied the M2 construct and performed MD simulations in M2TM or M2TM with amphipathic helices (M2AH). We also varied the lipid bilayer by changing either the lipid, DMPC or POPC, POPE or POPC/cholesterol (chol), or the lipids buffer size, 10x10 Å<sup>2 </sup>or 20x20 Å<sup>2</sup>. We aimed to suggest optimal system conditions for the computational description of this ion channel and related systems. Measures performed include quantities that are available experimentally and include: (a) the position of ligand, waters and chlorine anion inside the M2 pore, (b) the passage of waters from the outward Val27 gate of M2 S31N in complex with an aminoadamantane-aryl head blocker, (c) M2 orientation, (d) the AHs conformation and structure which is affected from interactions with lipids and chol and is important for membrane curvature and virus budding. In several cases we tested OPLS2005, which is routinely applied to describe drug-protein binding, and CHARMM36 which describes reliably protein conformation. We found that for the description of the ligands position inside the M2 pore, a 10x10 Å<sup>2</sup> lipids buffer in DMPC is needed when M2TM is used but 20x20 Å<sup>2</sup> lipids buffer of the softer POPC; when M2AH is used all 10x10 Å<sup>2</sup> lipid buffers with any of the tested lipids can be used. For the passage of waters at least M2AH with a 10x10 Å<sup>2</sup> lipid buffer is needed. The folding conformation of AHs which is defined from hydrogen bonding interactions with the bilayer and the complex with chol is described well with a 10x10 Å<sup>2</sup> lipids buffer and CHARMM36. </p>

scholarly journals Transmembrane signal transduction by cofactor transport

2021 ◽  
Author(s):  
Istvan Kocsis ◽  
Yudi Ding ◽  
Nicholas H. Williams ◽  
Christopher A. Hunter
Keyword(s):  
Signal Transduction ◽  
Lipid Bilayer ◽  
Metal Ion ◽  
Bilayer Membrane ◽  
Ester Hydrolysis ◽  
Lipid Bilayer Membrane ◽  
Metal Ion Cofactors

Synthetic transducers transport externally added metal ion cofactors across the lipid bilayer membrane of vesicles to trigger catalysis of ester hydrolysis in the inner compartment. Signal transduction activity is modulated by hydrazone formation.

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