Protein aggregates, self assembly

Li H, Bazan GC (2009) Conjugated oligoelectrolyte/ssDNA aggregates self-assembled multicomponent chromophores for protein discrimination. Adv Mater 21 964-967... 

DLS or SLS Presence of large aggregates/ impurities, determination of hydrodynamic radius of protein and self-assembly Can be performed using standalone dedicated instroments, or in a more basic way using fluorescence and UV spectrometers... 

Coacervation occurs in tropoelastin solutions and is a precursor event in the assembly of elastin nanofibrils [42]. This phenomenon is thought to be mainly due to the interaction between hydro-phobic domains of tropoelastin. In scanning electron microscopy (SEM) picmres, nanofibril stmc-tures are visible in coacervate solutions of elastin-based peptides [37,43]. Indeed, Wright et al. [44] describe the self-association characteristics of multidomain proteins containing near-identical peptide repeat motifs. They suggest that this form of self-assembly occurs via specific intermolecular association, based on the repetition of identical or near-identical amino acid sequences. This specificity is consistent with the principle that ordered molecular assembhes are usually more stable than disordered ones, and with the idea that native-like interactions may be generally more favorable than nonnative ones in protein aggregates. 

The information for proper aggregation of the protein subunits into the morphological units is contained within the structure of the subunits themselves, and the overall process of assembly is thus called self-assembly. A single virion generally has a large number of morphological units. 

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