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The classical version of the Kedem-Katchalsky equations is suitable for describing substance transport in membrane systems with well-stirred bathing solutions. However, when dealing with biological reality we are faced with a more complicated situation. For instance, in the living cell one can distinguish the central bulk area where the cytoplasm is well stirred due to its natural streaming and a certain relatively thin layer adjacent to the plasma membrane where there is no stirring. In such a situation, the passive transport of substance can be well described using the Kedem-Katchalsky equations in their more general form [1], The equations can, however, be applied provided the membrane boundary unstirred layers of cytoplasm are treated as diffusion layers. This has been shown in detail in the present work.
In this article the morphology of sarcoplasmic reticulum, classification of Ca2+ -ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+ -ATPase determined by electron and X-ray crystallog2r+aphy, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+ -ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+ -ATPase to the sarcoplasmic reticulum is discussed.
Over the last decade we have investigated the effects of cholesterol, polar carotenoids, and integral proteins (peptides) on the structure, dynamics, and hydrophobicity of saturated and unsaturated phosphatidylcholine (PC) membranes. The major results obtained in our studies can be summarized as follows: (1) The effect of unsaturation on the membrane alkyl chain order and reorientational motion is negligibly small; (2) The translational diffusion of lipids (lateral or vertical) as well as the diffusion of lipid-soluble small molecules is significantly decreased in cis- and trans-unsaturated PC membranes; (3) cis-unsaturated alkyl chains greatly decrease the ordering effect of membrane modifiers (cholesterol, polar carotenoids) as well as their effect on alkyl chain reorientational motion; (4) Introduction of a double bond into the alkyl chain increases the hydrophobicity (decreases water penetration) at all locations in the membrane; (5) Incorporation of cholesterol (30 mol%) decreases hydrophobicity (increases water penetration) from the polar headgroup region to a depth of approximately C7 and C9 for saturated and unsaturated PC membranes, respectively. Membrane hydrophobicity sharply increases at these positions from the level of methanol to the level of pure hexane, and hydrophobicity is constant in the inner region of the membrane.
The main structural element of biological membranes is a liquid-crystalline lipid bilayer. Other constituents, i.e. proteins, sterols and peptides, either intercalate into or loosely attach to the bilayer. We applied a molecular dynamics simulation method to study membrane systems at various levels of compositional complexity. The studies were started from simple lipid bilayers containing a single type phosphatidylcholine (PC) and water molecules (PC bilayers). As a next step, cholesterol (Chol) molecules were introduced to the PC bilayers (PC-Chol bilayers). These studies provided detailed information about the structure and dynamics of the membrane/water interface and the hydrocarbon chain region in bilayers built of various types of PCs and Chol. This enabled studies of membrane systems of higher complexity. They included the investigation of an integral membrane protein in its natural environment of a PC bilayer, and the antibacterial activity of magainin-2. The latter study required the construction of a model bacterial membrane which consisted of two types of phospholipids and counter ions. Whenever published experimental data were available, the results of the simulations were compared with them.
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