Proteins lipid environment

General anaesthetics have been in use for the last 100 years, yet their mechanism of action are still not yet clearly defined. For many years it was thought that general anaesthetics exerted their effects by dissolving in cell membranes and perturbing the lipid environment in a non-specific manner. This theory derived from the observation that for a number of drugs which induced anaesthesia, their potency correlated with their oil-water partition coefficients. This Meyer-Oveiton correlation was accepted for a number of years, however in the last 15-20 years evidence has shown that a more likely theory is that of specific interactions of anaesthetics with proteins, particularly those within the CNS that mediate neurotransmission [1]. 

Eleven controlled diet and environment experiments have been designed in a way that can be used to investigate the effects of protein nutrition and heat and/or water stress on diet-tissue A N. Laboratory rats were raised on purified, pelletized diets in which the isotopic composition of proteins, lipids and carbohydrates were well characterized and their proportions accurately and precisely measured (Ambrose and Norr 1993). Four experiments involved manipulation of temperature and/or water availability. Of these four experiments, one used a diet with high (70%) protein concentrations and heat/water stress (36°C) and three used normal (20%) protein concentrations. Seven experiments were conducted at normal temperature (21°C) with water ad libitum. Of these seven experiments, two used diets formulated with veiy low protein (5%), three with normal protein and two with high protein concentrations. 

To diffuse rapidly in the plane of the membrane (lateral diffusion), a molecule must simply move around in the lipid environment (including the polar head groups). It need not change how it interacts with phospholipids or with water since it is constantly exposed to pretty much the same environment. Lateral diffusion can be slowed (or prevented) by interactions between membrane proteins and the cellular cytoskeleton. This spatially restricts a plasma membrane protein to a localized environment. 

The introduced cysteine residues are found in one of three possible environments (1) on the water-accessible surface, (2) within the protein interior, or (3) at the protein-lipid interface (Karbn and Akabas, 1998). 

Vandenbussche G, Clercx A, Clercx M, et al. Secondary structure and orientation of the surfactant protein SP-B in a lipid environment. A Fourier transform infrared spectroscopy study. Biochemistry 1992 31(38) 9169-9176. 

R-groups, which act much like droplets of oil that coalesce in an aqueous environment. The nonpolar R-groups thus fill up the inte rior of the folded protein and help give it its three-dimensional shape. [Note In proteins that are located in a hydrophobic envi ronment, such as a membrane, the nonpolar R-groups are found on the outside surface of the protein, interacting with the lipid environment (see Figure 1.4).] The importance of these hydrophobic interactions in stabilizing protein structure is dis cussed on p. 19. 

Many of the proteins of membranes are enzymes. For example, the entire electron transport system of mitochondria (Chapter 18) is embedded in membranes and a number of highly lipid-soluble enzymes have been isolated. Examples are phosphatidylseiine decarboxylase, which converts phosphatidylserine to phosphatidylethanolamine in biosynthesis of the latter, and isoprenoid alcohol phosphokinase, which participates in bacterial cell wall synthesis (Chapter 20). A number of ectoenzymes are present predominantly on the outsides of cell membranes.329 Enzymes such as phospholipases (Chapter 12), which are present on membrane surfaces, often are relatively inactive when removed from the lipid environment but are active in the presence of phospholipid bilay-ers.330 33 The distribution of lipid chain lengths as well as the cholesterol content of the membrane can affect enzymatic activities.332... 

Biological membranes are always pictured as being very selective barriers separating different biochemical reaction compartments. This high performance transport specificity solely depends on the presence of membrane proteins embedded in the lipid matrix. On the other hand, most membrane proteins cease to function in the absence of lipids. In order to introduce biological transport abilities into artificial membrane systems protein-lipid interactions are of vital interest. The question is how the activity of membrane proteins is affected if they are placed into a polymeric environment. 

Biological Implications of Structural and Electrical Properties of Lipids. It is rather obvious that the structure of lipids is very important in connection with the function of living cells since most physiological processes occur in lipid environment. There is, for example, evidence that lipid-protein complexes are necessary for the proper functioning of mitochondria (56). Although lipids are most important in providing a suitable material for functional complexes (ionic channels, electron transport systems, receptor units, etc.), their own physical properties are certainly... 

Since DNA is a highly charged polyanion, it is always hydrated by water molecules [in the dry state (under moist air) it contains 12 water molecules per nucleotide subunit]. In a cellular environment, proteins (histones in eukaryotic cells) are always attached to DNA or are at least surrounded by proteins as in viruses. In order to attack DNA, radicals have to be sufficiently mobile in such a partially hydrophilic environment. For this reason, typical lipid radicals confined to the membranes will not be discussed here, although one must keep in mind that small fragments of free-radical nature maybe able to escape the lipid environment and can, in principle, also react with DNA. 

The conformation of proteins integrated into a membrane depends not only on the type and sequence of the amino adds but also on the lipid environment, i.e. the composition of the membrane. The effect of lipid environments and external factors such... 

Burdon542 has surveyed the current hypotheses for the structure of humic substances and has concluded that the various products from chemical degradations and NMR data are all consistent with their being mixtures of plant and microbial materials and their microbial degradation products. The examination of soil carbohydrates, proteins, lipids, and aromatics supported this view the presence of colour, fluorescence, ESR signals, mellitic acid, and other features do not contradict it. Regarding the Maillard reaction, some free monosaccharides and the necessary amino species are present in soil, so it may proceed, but only to a small extent it is not a major process. However, in marine environments, the relative abundance of carbohydrates and proteins makes them more probable precursors of humic substances than lignin or polyphenols. 

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