Molecular chaperones are essential for the correct folding of proteins in the cell under physiological and stress conditions. Two activities have been traditionally attributed to molecular chaperones: (1) preventing aggregation of unfolded polypeptides and (2) assisting in the correct refolding of chaperone-bound denatured polypeptides. We discuss here a novel function of molecular chaperones: catalytic solubilization and refolding of stable protein aggregates. In Escherichia coli, disaggregation is carried out by a network of ATPase chaperones consisting of a DnaK core, assisted by the Molecular weight marker proteins are routinely used in sodium dodecyl sulfate-polyacrylamide
gel electrophoresis to estimate the relative molecular mass of specific proteins
within a sample. This report describes a simple procedure for the generation of
multicolored molecular weight proteins using a variety of Remazol-reactive textile
dyes. These multicolored proteins provide a set of unambiguous markers for gel electrophoresis.
Furthermore, the colored markers can be used in conjunction with Western
blotting techniques to provide a visual display of marker proteins on the transfer
membrane.