A study of the native-denatured (N in equilibrium with D) transition in lysozyme. III. Effect of alteration of net charge by acetylation.
Measurement of the enzymic activity and fluorescence properties showed that the gross conformation of acetylated lysozyme [EC 3.2.1.17] is very similar to that of the native enzyme. On the other hand, protease digestion, t-butyl hypochloride modification and thermal denaturation experiments performed on native, acetylated, and guanidinated lysozymes showed that acetylation caused a small but significant shift of the N in equilibrium with D transition to the right. Thus it can be concluded that charge balance in a protein plays an important role in maintaining its conformation. The difference between equilibrium and kinetic methods of monitoring protein denaturation was also clarified.
D000107:Acetylation; D000117:Acetylglucosamine; D006146:Guanidines; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009113:Muramidase; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D013381:Subtilisins
D006146:Guanidines; D009113:Muramidase; D013381:Subtilisins; D000117:Acetylglucosamine