Aggregates shell-like

It is pertinent to note here the observed increase in the value of the structure-sensitive parameter p from 1 to 2. This implies that the architecture of the sodium caseinate aggregates, as modified by interaction with the surfactant, becomes generally more open, despite the inferred collapse of their constituent protein nanoparticles. In contrast, a shell-like aggregation structure can be inferred for the self-assembly of sodium caseinate as a result of its interaction with the non-ionic surfactant PGE (this surfactant is based on a mixture of the esters of stearic and palmitic acids in chemical combination with polyglycerol (Krog, 1997)). 

Experiments made at higher degrees of aggregation have provided strong evidence192 for ring-like structures for mixed neutral clusters. For example, under a wide variety of experimental conditions, mixed cluster ions display a maximum intensity atm = 2(n + 1) whenn<5 for (NH3)II (M)mH+, andm = n + 2 whenn<4 for (H20)B(M)mH+ M is a proton acceptor such as acetone, pyridine, and trimethy-lamine. These findings reveal that the cluster ions with these compositions have stable solvation shell structures as discussed above. 

It was shown by McClain et al. that a series of PS- -PFOA copolymers studied by SANS and SAXS form polydisperse spherical core-shell micelles, where PS forms the spherical core and PFOA forms the corona, or shell, swollen with C02 (Londono et al., 1997 McClain et al., 1996b). In most cases, the core radius was 25 A, the shell radius was 85 A, and the aggregation number was 7. With an increase in C02 density implemented by decreasing the temperature, the polydispersity increased, likely from breaking a collection of aggregates of low polydispersity into a collection of smaller aggregates of higher polydispersity. 

Some attention should be also paid to the fact that some copolymers with special sequence distribution do not assume cylindrical shape within the HA model. For example, this is the case for protein-like sequences. Protein-like sequences correspond to a copolymer which forms globules with a hydrophobic core and a hydrophilic shell showing no tendency to aggregation. Proteinlike copolymers have been previously studied within the HP model [32-34], Application of the more realistic HA model showed that the globules formed by protein-like copolymers under worsening solvent quality assume conventional spherical shape and show no tendency to aggregate [23]. The stability for HA model protein-like copolymers is much higher than for those within the HP model. 

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