Protein-vesicle interaction

Protein-lipid interaction in retinal-rod outer disc membranes in sonicated vesicles is suggested from comparison of the T1 data of these vesicles with those of extracted liposome preparations from the same source (Brown et al., 1976). Chloroplast thylakoids form micellar structures in chloroform and bilayer structures in water. It was shown by 13C relaxation (Johns et al., 1977) that T1 data are sensitive to this change in secondary structure. As in the... 

Vesicles have demonstrated their dynamic behaviour in studies showing evidence of rapid domain formation in response to external stimuli [9], The binding of glycosidic domains to cholera toxin has been demonstrated using vesicles as biomimetic sensors [99], Protein-carbohydrate interaction has also been studied using synthetic glycolipids recently by Barboiu et al. [100] (Fig. 5). 

When an action potential approaches the axon terminal, voltage-gated Ca2+ channels (N-type) open and Ca2+ enters the presynapse. Ca2+ ions bind to proteins that connect the synaptic vesicle with the plasma membrane (acronym SNAP), inducing membrane fusion and consequently exocytosis of the neurotransmitter into the synaptic cleft. Botulinum b toxin contains a specific protease which interferes with synaptobrevin (a vesisle protein which interacts with the SNAP proteins) so that vesicles cannot fuse any longer. The inhibition of acetylcholine release can thus cause paralysis and death. 

Therefore, to understand the behavior of food emulsions, we need to know as much as possible about these types of emulsifiers, because fliey may not behave exactly similarly to classical small-molecule emulsifiers. For example, phospholipid molecules can interact with each other to form lamellar phases or vesicles they may interact with neutral lipids to form a mono- or multi-layer around the lipid droplets, or they may interact with proteins which are either adsorbed or free in solution. Any or all of these interactions may occur in one food emulsion. The properties of the emulsion system depend on which behavior pattern predominates. Unfortunately for those who have to formulate food emulsions, it is rarely possible to consider the emulsion simply as oil coated with one or a mixture of surfactants. Almost always there are other components whose properties need to be considered along with those of the emulsion droplets themselves. For example, various metal salts may be included in the formulation (e.g. Ca " is nearly always present in food products derived from milk ingredients), and there may also be hydrocolloids present to increase the viscosity or yield stress of the continuous phase to delay or prevent creaming of the emulsion. In addition, it is very often the case, in emulsions formulated using proteins, that some of the protein is free in solution, having either not adsorbed at all or been displaced by other surfactants. Any of these materials (especially the metal salts and the proteins) may interact with the molecules... 

Hydrogen Exchange Mass Spectrometry of Membrane Proteins 281 16.2.2 Myoglobin-Vesicle Interaction... 

Broos, J, ter Veld, F, and RobiUard, GT, Membrane protein-hgand interactions in Escherichia coh vesicles and living cells monitored via a biosyntheticaUy incorporated tryptophan iTi3[ogue. Biochemistry 3S (1999) 9798-9803. 

Went, M. R., and De Camilli, P. (2004). Protein-lipid interactions and phosphoinositide metabolism in membrane traffic Insights from vesicle recycling in nerve terminals. Proc. Natl Acad. Scl USA 101, 8262-8269. 

Lesa, G. M., Seemann, J., Shorter, J., Vandekerckhove, J., and Warren, G. (2000). The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein pll5. J. Biol. Chem. 275, 2831-2836. 

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