Weakly charged proteins

The list of the new gels for which phase transitions are possible is supplemented in the paper by Amiya and Tanaka, who discovered discrete collapse for the most important representatives of biopolymers - chemically crosslinked networks formed by proteins, DNA and polysaccharides [45]. Thus, it was demonstrated that discrete collapse is a general property of weakly charged gels and that the most important factor, which is responsible for the occurrence of this phenomenon, is the osmotic pressure of the system of counter ions. 

Answer Protein C has a net negative charge because there are more Glu and Asp residues than Lys, Arg, and His residues. Protein A has a net positive charge. Protein B has no net charge at neutral pH. A cation-exchange column has a negatively charged polymer, so protein C interacts most weakly with the column and is eluted first, foUowed by B, then A. 

At the second critical pH (pH,, ), which is usually below the protein isoelectric point, strong electrostatic interaction between positively charged protein molecules and anionic polysaccharide chains will cause soluble protein/polysaccharide complexes to aggregate into insoluble protein/polysaccharide complexes. For negatively charged weak acid-based (e.g., carboxylic acid) polysaccharides like pectin, with the decrease of pH below the pKa of the polysaccharide, protein (e.g., bovine serum albumin (BSA))/polysaccharide (e.g., pectin) insoluble complexes may dissociate into soluble complexes, or even non-interacted protein molecules and polysaccharide chains, due to the low charges of polysaccharide chains as well as the repulsion between the positively charged proteins (Dickinson 1998). 

Cold-soluble gelatins (SF), produced by enzymic hydrolysis, have a very weak charge, a low peptide content and lightweight proteins M < 10 ... 

Because water-water hydrogen bonds are relatively weak, the influence of a single protein surface charge diminishes with distance from the charge. Proteins, however, pack many surface charges into a dense region. 

If the molecule of interest is neutral or weakly charged then the sample can be analyzed directly without removing the protein or any treatment using MEKC. Analysis by MEKC can tolerate proteins since the surfactants in the MEKC solubilize them. 

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