An electrochemical investigation of ligand-binding abilities of film-entrapped myoglobin.
Film-entrapped myoglobin exhibits well-defined electrochemistry which, upon ligand binding, displays a titratable redox potential shift. This effect has been observed to be highly dependent on the charged state of involved films. We have demonstrated that this approach may act as a model system for studies of molecular recognition between proteins and ligands.
Zhang
Wenjun
W
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, PR China.
Fan
Chunhai
C
Sun
Yuting
Y
Li
Genxi
G
D000077286:Cetrimonium; D002593:Cetrimonium Compounds / Q000737:chemistry; D004247:DNA / Q000737:chemistry; D004563:Electrochemistry / Q000379:methods*; D007093:Imidazoles / Q000737:chemistry*; D008024:Ligands; D046911:Macromolecular Substances; D008567:Membranes, Artificial; D009211:Myoglobin / Q000737:chemistry*; D010084:Oxidation-Reduction; D010713:Phosphatidylcholines / Q000737:chemistry; D011094:Polyethyleneimine / Q000737:chemistry; D011485:Protein Binding; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry
D002593:Cetrimonium Compounds; D007093:Imidazoles; D008024:Ligands; D046911:Macromolecular Substances; D008567:Membranes, Artificial; D009211:Myoglobin; D010713:Phosphatidylcholines; D012967:Sodium Dodecyl Sulfate; C029899:imidazole; D011094:Polyethyleneimine; D004247:DNA; D000077286:Cetrimonium