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Permeation of Organometallic Compounds through Phospholipid Membranes

von Dr. Raycho Yonchev

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[1.] Ry/Fragment 008 01 - Diskussion
Zuletzt bearbeitet: 2016-01-27 10:49:32 Klgn
Anézo 2003, Fragment, Gesichtet, KomplettPlagiat, Ry, SMWFragment, Schutzlevel sysop

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They can be differentiated by two main features – the size and electrical property of the headgroups, which may be charged, zwiterioninc [sic], or neutral, and the structure of the hydrocarbon chains which may have various lengths and different degrees of unsaturation. It should be emphasized that lipids having the same polar headgroup but different hydrocarbon chains, or vice versa, exhibit different physical and metabolic properties. The various membranes present in different organisms show characteristic patterns of lipid composition. To a first approximation, the specific functions exhibited by these membranes may arise from qualitative and quantitative differences an [sic] their composition. Many of these functions, however, might be appreciated in terms of the properties of the membrane in specific environments and not on the basis of the structure or the reactivity of its components per-se [sic] [2].

Membranes contain between 20 and 80 weight percent protein. Just as each membrane can be characterized by its lipid composition, each membrane can also be characterized by its protein contents. Thousands of different proteins are found as constituents of biological membranes. Whereas the primary role of membrane lipids is to provide the structural framework of the membrane in the form of stable bilayers, proteins provide the diversity of enzymes, transporters, receptors, and pores, i.e. the principal active components of the membrane. The covalent structure of the membrane proteins is similar to that of soluble proteins. Membrane proteins can be distinguished from non-membranous proteins by the nature of their association with the lipid bilayers. This association may be loose or tight. The proteins may be incorporated into the bilayers structure or simply associated to a lipid or protein component on the surface of the membrane. Membrane proteins are generally bound to the membrane through non-covalent forces, such as the hydrophobic force or electrostatic interactions. They may fold so as to present both a non-polar hydrophobic surface, which can interact with the apolar regions of the lipid bilayers, and polar or charged regions which can interact with the polar lipid headgroups at the interface of the membrane. There is also a certain number of membrane proteins which are covalently bound to the membrane via lipid anchors. Operationally, membrane proteins have been divided into two major classes – [peripheral (or extrinsic) proteins and integral (or intrinsic) proteins.]


2. Jain, M. K. Introduction to Biological Membranes, 2nd ed.; John Wiley & Sons: New York, 1988.

They can be differentiated by two main features: the size and electrical property of the headgroups which may be charged, zwitterionic, or neutral, and the structure of the hydrocarbon chains which may have various lengths and different degrees of unsaturation. It should be emphasized that lipids having the same polar headgroup but different hydrocarbon chains, or vice versa, exhibit different physical and metabolic properties.

The various membranes present in different organisms show characteristic patterns of lipid composition. To a first approximation, the specific functions exhibited by these membranes may arise from qualitative and quantitative differences in their composition. Many of these functions, however, might be appreciated in terms of the properties of the membrane in specific environments and not on the basis of the structure or the reactivity of its components per se [4].

[page 21:]

1.1.2.2 Membrane proteins

Membranes contain between 20 and 80 weight% protein. Just as each membrane can be characterized by its lipid composition, each membrane can be also characterized by its protein content. Thousands of different proteins are found as constituents of biological membranes. Whereas the primary role of membrane lipids is to provide the structural framework of the membrane in the form of a stable bilayer, proteins provide the diversity of enzymes, transporters, receptors, and pores, i.e. the principal active components of the membrane.

The covalent structure of membrane proteins is similar to that of soluble proteins. Membrane proteins can be distinguished from non-membranous proteins by the nature of their association with the lipid bilayer. This association may be loose or tight. The proteins may be incorporated into the bilayer structure or simply associated to a lipid or protein component on the surface of the membrane. Membrane proteins are generally bound to the membrane through non-covalent forces, such as the hydrophobic force or electrostatic interactions. They may fold so as to present both a non-polar hydrophobic surface which can interact with the apolar regions of the lipid bilayer, and polar or charged regions which can interact with the polar lipid headgroups at the interface of the membrane. There is also a certain number of membrane proteins which are covalently bound to the membrane via lipid anchors.

Operationally, membrane proteins have been divided into two major classes: peripheral (or extrinsic) proteins and integral (or intrinsic) proteins.


[4] M. K. Jain. Introduction to Biological Membranes. John Wiley & Sons, New York, second edition, 1988.

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