scholarly journals Lipid-Dependent Effects of Halothane on Gramicidin Channel Kinetics: A New Role for Lipid Packing Stress

Biochemistry ◽  
2009 ◽  
Vol 48 (24) ◽  
pp. 5501-5503 ◽  
Author(s):  
Michael Weinrich ◽  
Tatiana K. Rostovtseva ◽  
Sergey M. Bezrukov
Keyword(s):  
Channel Kinetics ◽  
Lipid Packing ◽  
Gramicidin Channel

scholarly journals Gramicidin Channel Kinetics under Tension

1998 ◽  
Vol 74 (1) ◽  
pp. 328-337 ◽  
Author(s):  
M. Goulian ◽  
O.N. Mesquita ◽  
D.K. Fygenson ◽  
C. Nielsen ◽  
O.S. Andersen ◽  
...  
Keyword(s):  
Channel Kinetics ◽  
Gramicidin Channel

scholarly journals Interfacial Polar Interactions Affect Gramicidin Channel Kinetics

2008 ◽  
Vol 94 (4) ◽  
pp. L23-L25 ◽  
Author(s):  
Tatiana K. Rostovtseva ◽  
Horia I. Petrache ◽  
Namdar Kazemi ◽  
Elnaz Hassanzadeh ◽  
Sergey M. Bezrukov
Keyword(s):  
Channel Kinetics ◽  
Gramicidin Channel ◽  
Polar Interactions

Penetration and preferential binding of charged nanoparticles to mixed lipid monolayers: interplay of lipid packing and charge density

Soft Matter ◽  
2020 ◽  
Author(s):  
Anurag Chaudhury ◽  
Koushik Debnath ◽  
Wei Bu ◽  
Nikhil R. Jana ◽  
Jaydeep Kumar Basu
Keyword(s):  
Charge Density ◽  
Biomedical Applications ◽  
Cell Membranes ◽  
Lipid Monolayers ◽  
Cytotoxic Effects ◽  
Lipid Packing ◽  
Preferential Binding ◽  
Charged Nanoparticles

Designing of nanoparticles (NPs) for biomedical applications or mitigating their cytotoxic effects require microscopic understanding of their interactions with cell membranes. Such insight is best obtained by studying model biomembranes...

Memory in Ion Channel Kinetics

2021 ◽  
Author(s):  
M. P. Silva ◽  
C. G. Rodrigues ◽  
W. A. Varanda ◽  
R. A. Nogueira
Keyword(s):  
Ion Channel ◽  
Channel Kinetics ◽  
Ion Channel Kinetics

Specificity and promiscuity in membrane helix interactions

1994 ◽  
Vol 27 (2) ◽  
pp. 157-218 ◽  
Author(s):  
Mark A. Lemmon ◽  
Donald M. Engelman
Keyword(s):  
Membrane Proteins ◽  
Transmembrane Helix ◽  
Integral Membrane Proteins ◽  
Lipid Packing ◽  
Membrane Protein Folding ◽  
Membrane Spanning ◽  
Α Helix ◽  
Prosthetic Groups ◽  
Packing Effects ◽  
Helix Interactions

The membrane-spanning portions of many integral membrane proteins consist of one or a number of transmembrane α-helices, which are expected to be independently stable on thermodynamic grounds. Side-by-side interactions between these transmembrane α-helices are important in the folding and assembly of such integral membrane proteins and their complexes. In considering the contribution of these helix–helix interactions to membrane protein folding and oligomerization, a distinction between the energetics and specificity should be recognized. A number of contributions to the energetics of transmembrane helix association within the lipid bilayer will be relatively non-specific, including those resulting from charge–charge interactions and lipid–packing effects. Specificity (and part of the energy) in transmembrane α-helix association, however, appears to rely mainly upon a detailed stereochemical fit between sets of dynamically accessible states of particular helices. In some cases, these interactions are mediated in part by prosthetic groups.

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