Renaturation of lysozyme with assistance of artificial chaperone;

Influencing factors in the refolding process of artificial molecular chaperone assisting chicken IL-18 recombination protein

Cooperation of osmolytes and artificial chaperone on malate dehydrogenase refolding;

The effect of guanidine hydrochloride (GuHCl) concentration on the oxidative refolding of denatured-reduced lysozyme of high concentration in the presence of artificial chaperone, that is, cetyl trimethyl ammonium bromide (CTAB) and β -cyclodextrin ( β -CD),was studied.

A kinetic model based on the competition between protein folding and aggregation was employed to express the refolding process of denatured/reduced lysozyme by direct dilution and that facilitated by the artificial chaperone system (ACS), i.

Renaturation of high concentration lysozyme using gel filtration chromatography assisted by artificial chaperones;

In order to explore the best concentration of glutathione in the test assisting with artificial chaperones by one-step method,the hydrochloric acid-Denatured and DTT-Reduced Lysozyme are taken as the model protein.

Based on the improvement of measuring the standard curve of lysozyme activity, we optimized the conditions of the lysozyme refolding assisted by artificial chaperones.

Effect of ATP on molecular chaperone function and conformation of α-crystallin;

Change of molecular chaperone activity of high-molecular-weight alpha-crystallin in age-related cataract;

Effects of fructose 6-phosphate and ribose on molecular chaperone activity of α-crystallin;

They work as chaperones participating in the folding and unfolding,assembly of multisubunit complexes, transportation and degradation of proteins and play an important role in biochemical function of proteins.

The properly folding of most heterologous proteins need the helper molecular chaperones.