Proteins confirmational behavior

This comparative study pointed out molecular close packing as a key parameter responsible for the thermal stability of proteins in films. In the case of BR, this close packing is reached due to the nature of the sample, while LB organization seems to be a more general procedure, for the same goal can be reached for practically any type of protein sample. The last statement was even confirmed by the comparison of the thermal behavior of extracted separated BR in self-assembled and LB films. It was found that BR in LB films is more stable for this kind of sample. The results will be reported in detail elsewhere. 

Reports that AA is released primarily by G-protein-mediated PLA2 activation remain to be confirmed [84, 85]. In addition, modulation of PLA2 by Ca2+ and protein kinase needs to be better defined. It is clear that NMDA receptor activation promotes the release of AA [86], and that a variety of eicosanoids are then generated (Fig 33-2,33-3). The modulatory events that channel AA towards specific eicosanoids are not understood. The endocannabinoid family of lipid messengers will remain an active focus of interest because of the growing evidence of their actions in synaptic function, learning, memory, and other forms of behavior [56,87]. 

Let us turn our attention back again to the scheme illustrating various versions of the joint application of fluorescence parameters (Figure 2.1) and consider the possibilities for constructing more general and more definite models of protein dynamics. These models can be suggested and confirmed or rejected by comparing predicted behavior with the results of spectroscopic experiments of different kinds. 

Displacement of the protein from the adsorbed layer in o/w thin films shows very different behavior from its a/w counterpart. Although displacement of protein from the o/w interfaces initiates at approximately the same solution composition (i.e., R = 0.1), there is little evidence for the stepwise displacement observed in the a/w thin films. This observation is further confirmation of the monolayer versus multilayer structure at the o/w and a/w thin films. The displacement of /3-lg has also been investigated in oil-in-water emulsions of n-tetradecane [46,47], In these reports it was shown that the protein was not completely displaced until R = 10, which was considerably higher than R = 1 - 2 in Figure 22. This will be discussed further below. 

A surface or interface can influence the assembly of fibrils by altering both the process and kinetics of fibril nucleation or elongation. This behavior is not surprising as surface properties are known to influence the absorption, confirmation, and destabilization of globular proteins or smaller peptides (Rocha et al., 2005). Surface properties influence fibril assembly in a similar way by altering the absorption, unfolding, and aggregation of monomers. 

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