ISSN:
1432-1017
Keywords:
Lipid-protein bilayers
;
Permeability
;
Computer simulation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
Abstract We have modelled the effect of integral proteins upon the permeability of a lipid bilayer membrane to small ions. Our intention is to predict the temperature-and protein concentration-dependence of the relative ionic diffusion coefficient if it is assumed that the ions diffuse entirely through the lipid regions of the membrane, and do not cross the bilayer either by moving through the protein or along its hydrophobic surface. We used models of lipid-protein bilayers that have been used successfully before, together with a modification of the (protein-free) permeability mechanism of Kanchisa, Tsong, Cruzeiro-Hansson and Mouritsen (KTCM). We used Monte Carlo techniques to simulate the thermodynamics and permeability of the membrane because such a calculation, which depends upon spatial and time correlations, cannot be done using a mean field approximation. We took the protein to be analogous to bacteriorhodopsin and calculated the relative diffusion coefficients, R, of small ions through a DMPC bilayer containing such proteins. We found that although there is only a small change in R when T 〉 T m , R can change by an order of magnitude, depending upon the protein concentration, for T 〈 T m . We showed that regions of largest lipid area fluctuations and, hence, compressibility occur (i) at the interfaces between regions (which may be very small and not macroscopic phases) of extended-chain and excited-chain lipids, thus showing the similarity between this model and the KTCM model, and (ii) in regions where the temperature is close to T m but the lipids are prevented from becoming ordered because of the proximity of proteins which try to keep them in their excited-chain states. We have plotted lipid fluctuation and ionic permeability maps to show which regions of the membrane display the largest permeability, and we show how these regions change as a function of temperature.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00183378
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