1996, pp 405-462

Thermodynamics of the Interaction of Proteins with Lipid Membranes

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Abstract

Peripheral proteins associated at the lipid surface are one of the major components of biological membranes. They may function in situ as electron carriers (e.g., cytochrome c), as enzymes (e.g., protein kinase C), as signal transduction proteins (e.g., G-proteins), or primarily as structural elements (e.g., spectrin and myelin basic protein). The protein density at the membrane surface can be relatively high, and the peripheral proteins may also interact with the exposed portions of integral proteins embedded within the membrane (e.g., with redox enzymes of the respiratory chain, or with receptors such as those to which G-proteins are coupled). The association with the membrane is most frequently of electrostatic origin but may also include surface adsorption and hydrophobic components. The interactions of the isolated peripheral proteins with lipid bi-layer membranes, therefore, are of direct relevance to the structure and function of biological membranes, and the determination of binding isotherms has proved to be particularly useful in the study of such interactions. Analysis of the latter constitutes the first and an important part of this chapter that is directly relevant to the thermodynamics of binding.