7. Collective dynamics in lipid membranes

2011 ◽  
Vol 83 (5) ◽  
Author(s):  
Martin D. Kaye ◽  
Karin Schmalzl ◽  
Valeria Conti Nibali ◽  
Mounir Tarek ◽  
Maikel C. Rheinstädter

2016 ◽  
Vol 110 (3) ◽  
pp. 369a
Author(s):  
Soohyun K. Lee ◽  
Trivikram R. Molugu ◽  
K.J. Mallikarjunaiah ◽  
Michael F. Brown

2004 ◽  
Vol 93 (10) ◽  
Author(s):  
M. C. Rheinstädter ◽  
C. Ollinger ◽  
G. Fragneto ◽  
F. Demmel ◽  
T. Salditt

Soft Matter ◽  
2021 ◽  
Author(s):  
Elizabeth G. Kelley ◽  
Paul D. Butler ◽  
Michihiro Nagao

Small amounts of transmembrane peptides can significantly alter the collective dynamics in lipid membranes even when there are no changes in the average membrane structure.


1997 ◽  
Vol 161 ◽  
pp. 437-442
Author(s):  
Salvatore Di Bernardo ◽  
Romana Fato ◽  
Giorgio Lenaz

AbstractOne of the peculiar aspects of living systems is the production and conservation of energy. This aspect is provided by specialized organelles, such as the mitochondria and chloroplasts, in developed living organisms. In primordial systems lacking specialized enzymatic complexes the energy supply was probably bound to the generation and maintenance of an asymmetric distribution of charged molecules in compartmentalized systems. On the basis of experimental evidence, we suggest that lipophilic quinones were involved in the generation of this asymmetrical distribution of charges through vectorial redox reactions across lipid membranes.


Author(s):  
Neng-Bo He ◽  
S.W. Hui

Monolayers and planar "black" lipid membranes have been widely used as models for studying the structure and properties of biological membranes. Because of the lack of a suitable method to prepare these membranes for electron microscopic observation, their ultrastructure is so far not well understood. A method of forming molecular bilayers over the holes of fine mesh grids was developed by Hui et al. to study hydrated and unsupported lipid bilayers by electron diffraction, and to image phase separated domains by diffraction contrast. We now adapted the method of Pattus et al. of spreading biological membranes vesicles on the air-water interfaces to reconstitute biological membranes into unsupported planar films for electron microscopic study. hemoglobin-free human erythrocyte membrane stroma was prepared by hemolysis. The membranes were spreaded at 20°C on balanced salt solution in a Langmuir trough until a surface pressure of 20 dyne/cm was reached. The surface film was repeatedly washed by passing to adjacent troughs over shallow partitions (fig. 1).


Author(s):  
S. W. Hui ◽  
T. P. Stewart

Direct electron microscopic study of biological molecules has been hampered by such factors as radiation damage, lack of contrast and vacuum drying. In certain cases, however, the difficulties may be overcome by using redundent structural information from repeating units and by various specimen preservation methods. With bilayers of phospholipids in which both the solid and fluid phases co-exist, the ordering of the hydrocarbon chains may be utilized to form diffraction contrast images. Domains of different molecular packings may be recgnizable by placing properly chosen filters in the diffraction plane. These domains would correspond to those observed by freeze fracture, if certain distinctive undulating patterns are associated with certain molecular packing, as suggested by X-ray diffraction studies. By using an environmental stage, we were able to directly observe these domains in bilayers of mixed phospholipids at various temperatures at which their phases change from misible to inmissible states.


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