摘要
Azurins, a wild type and a genetically mutant K27 altered one, were immobilized on annealed gold surface and investigated by means of atomic force microscopy. It was found that the surface coverage and height distribution of the adsorbed protein molecules are different from each other, which is possibly the result of the different orientation on the surface. It is believed that the wild type azurin is connected to gold surface by the disulphide bridge; while the mutant, K27C, might be through the thiol groups of the cysteine residues on their surface.
Azurins, a wild type and a genetically mutant K27 altered one, were immobilized on annealed gold surface and investigated by means of atomic force microscopy. It was found that the surface coverage and height distribution of the adsorbed protein molecules are different from each other, which is possibly the result of the different orientation on the surface. It is believed that the wild type azurin is connected to gold surface by the disulphide bridge; while the mutant, K27C, might be through the thiol groups of the cysteine residues on their surface.
