Like charges repel. A peptide carrying net charge resists aggregating with its neighbours and stays in solution; one at its isoelectric point, where positive and negative balance to zero, has lost that repulsion and is at its least soluble.
This is why the same peptide can dissolve readily in one diluent and poorly in another at a different pH, with nothing else changed.
Sequences rich in residues such as leucine, isoleucine, valine and phenylalanine have surfaces that water accommodates poorly, and those surfaces prefer each other. The result is slow dissolution, cloudiness, or material that appears to dissolve and then comes back out.
That is a property of the sequence, not a defect in the lot. A certificate reports identity and purity; it does not promise that a given diluent will suit a given sequence.
A solution that stays hazy after gentle swirling contains undissolved or aggregated material, and the concentration is therefore lower than the calculation assumed. Proceeding on the assumed figure is how an experiment quietly runs at the wrong concentration.
Swirl rather than shake — particularly for a folded protein, where agitation drives material to the air-liquid interface and promotes the aggregation being diagnosed.
Like charges repel. A peptide carrying net charge resists aggregating with its neighbours and stays in solution; one at its isoelectric point, where positive and negative balance to zero, has lost that repulsion and is at its least soluble.
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