Nanomechanical properties of lipid bilayer: Asymmetric modulation of lateral pressure and surface tension due to protein insertion in one leaflet of a bilayer

2013 ◽  
Vol 138 (6) ◽  
pp. 065101 ◽  
Author(s):  
Negin Maftouni ◽  
Mehriar Amininasab ◽  
Mohammad Reza Ejtehadi ◽  
Farshad Kowsari ◽  
Reza Dastvan
Keyword(s):  
Surface Tension ◽  
Lipid Bilayer ◽  
Lateral Pressure ◽  
Protein Insertion ◽  
Nanomechanical Properties ◽  
Asymmetric Modulation

Molecular dynamics study of gramicidin a in lipid bilayer: Structure and lateral pressure profile

2012 ◽  
Vol 112 (24) ◽  
pp. 3834-3839 ◽  
Author(s):  
Hiroaki Saito ◽  
Masashi Iwayama ◽  
Hiroyuki Takagi ◽  
Megumi Nishimura ◽  
Takeshi Miyakawa ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Lipid Bilayer ◽  
Lateral Pressure ◽  
Pressure Profile ◽  
Gramicidin A ◽  
Bilayer Structure ◽  
Lateral Pressure Profile

A Molecular Dynamics Simulation Study of Nanomechanical Properties of Asymmetric Lipid Bilayer

2012 ◽  
Vol 246 (1) ◽  
pp. 67-73 ◽  
Author(s):  
Negin Maftouni ◽  
Mehriar Amininasab ◽  
Mansour Vali ◽  
Mohammadreza Ejtehadi ◽  
Farshad Kowsari
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Lipid Bilayer ◽  
Simulation Study ◽  
Dynamics Simulation ◽  
Nanomechanical Properties

scholarly journals Lateral pressure profile in bent lipid membranes and mechanosensitive channels gating

2016 ◽  
Author(s):  
Anna A. Drozdova ◽  
Sergei I. Mukhin
Keyword(s):  
Pressure Distribution ◽  
Lipid Bilayer ◽  
Lateral Pressure ◽  
Small Deviation ◽  
Finite Thickness ◽  
Analytical Calculation ◽  
Pressure Profile ◽  
Entropic Repulsion ◽  
Bending Modulus ◽  
Lateral Pressure Profile

AbstractThis review describes the analytical calculation of lateral pressure profile in the hydrophobic part of the lipid bilayer with finite curvature based on previously developed microscopic model for lipid hydrocarbon chains. According to this theory the energy per unit chain is represented as energy of flexible string (Euler’s elastic beam of finite thickness) and interaction between chains is considered as an entropic repulsion. This microscopic theory allows to obtain expression for lateral pressure distribution in bent bilayer if treating a bending as a small deviation from the flat membrane conformation and using perturbation theory. Because lateral pressure distribution is related to elastic properties of lipid bilayer then the first moment of lateral pressure and the expression for bending modulus may be derived from this theoretical model. Finally one can estimate the energy difference between two various conformational states of mechanosensitive channel embedded into the bilayer with pressure profile Пt(z).

scholarly journals FCS Study of the Thermodynamics of Membrane Protein Insertion into the Lipid Bilayer Chaperoned by Fluorinated Surfactants

2008 ◽  
Vol 95 (8) ◽  
pp. L54-L56 ◽  
Author(s):  
Yevgen O. Posokhov ◽  
Mykola V. Rodnin ◽  
Somes K. Das ◽  
Bernard Pucci ◽  
Alexey S. Ladokhin
Keyword(s):  
Membrane Protein ◽  
Lipid Bilayer ◽  
Fluorinated Surfactants ◽  
Protein Insertion ◽  
Membrane Protein Insertion

Simulation of a fluid phase lipid bilayer membrane: Incorporation of the surface tension into system boundary conditions

1995 ◽  
Vol 5 (1-3) ◽  
pp. 45-53
Author(s):  
S. -W. Chiu ◽  
M. Clark ◽  
V. Balaji ◽  
S. Subramaniam ◽  
H. L. Scott ◽  
...  
Keyword(s):  
Surface Tension ◽  
Boundary Conditions ◽  
Lipid Bilayer ◽  
Fluid Phase ◽  
Bilayer Membrane ◽  
Lipid Bilayer Membrane ◽  
System Boundary

Front propagation in laser-tweezed lipid bilayer tubules

1996 ◽  
Vol 463 ◽  
Author(s):  
Peter D. Olmsted ◽  
Fred C. Mackintosh
Keyword(s):  
Surface Tension ◽  
Boundary Conditions ◽  
Lipid Bilayer ◽  
Control Parameter ◽  
Laser Intensity ◽  
Front Propagation ◽  
Chemical Potentials ◽  
Unstable Medium ◽  
Lipid Tubules ◽  
Correct Boundary Conditions

AbstractWe study the mechanism of the ‘pearling’ instability seen recently in experiments on lipid tubules under a local applied laser intensity. We argue that the correct boundary conditions are fixed chemical potentials, or surface tensions Σ, at the laser spot and the reservoir in contact with the tubule. While most qualitative conclusions of previous studies remain the same, the ‘ramped’ control parameter (surface tension) implies several new features. We also explore some consequences of front propagation into a noisy unstable medium.

scholarly journals Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein

2018 ◽  
Vol 115 (8) ◽  
pp. E1799-E1808 ◽  
Author(s):  
M. R. Sanders ◽  
H. E. Findlay ◽  
P. J. Booth
Keyword(s):  
Free Energy ◽  
Lipid Bilayer ◽  
Lipid Bilayers ◽  
Thermodynamic Stability ◽  
Lateral Pressure ◽  
Helical Structure ◽  
Free Energies ◽  
Transport Activity ◽  
Helical Protein ◽  
Urea Unfolding

α-Helical membrane proteins have eluded investigation of their thermodynamic stability in lipid bilayers. Reversible denaturation curves have enabled some headway in determining unfolding free energies. However, these parameters have been limited to detergent micelles or lipid bicelles, which do not possess the same mechanical properties as lipid bilayers that comprise the basis of natural membranes. We establish reversible unfolding of the membrane transporter LeuT in lipid bilayers, enabling the comparison of apparent unfolding free energies in different lipid compositions. LeuT is a bacterial ortholog of neurotransmitter transporters and contains a knot within its 12-transmembrane helical structure. Urea is used as a denaturant for LeuT in proteoliposomes, resulting in the loss of up to 30% helical structure depending upon the lipid bilayer composition. Urea unfolding of LeuT in liposomes is reversible, with refolding in the bilayer recovering the original helical structure and transport activity. A linear dependence of the unfolding free energy on urea concentration enables the free energy to be extrapolated to zero denaturant. Increasing lipid headgroup charge or chain lateral pressure increases the thermodynamic stability of LeuT. The mechanical and charge properties of the bilayer also affect the ability of urea to denature the protein. Thus, we not only gain insight to the long–sought-after thermodynamic stability of an α-helical protein in a lipid bilayer but also provide a basis for studies of the folding of knotted proteins in a membrane environment.

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