Interactions between cysteine residues as probes of protein conformation: the disulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitor.
Creighton, T E
Interactions between cysteine residues as probes of protein conformation: the disulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitor. [electronic resource] - Journal of molecular biology Aug 1975 - 767-76 p. digital
Publication Type: Journal Article
0022-2836
10.1016/0022-2836(75)90151-5 doi
Animals
Binding Sites
Cysteine--analysis
Disulfides--analysis
Dithiothreitol
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Pancreas
Protein Binding
Thermodynamics
Trypsin Inhibitors--analysis
Interactions between cysteine residues as probes of protein conformation: the disulphide bond between Cys-14 and Cys-38 of the pancreatic trypsin inhibitor. [electronic resource] - Journal of molecular biology Aug 1975 - 767-76 p. digital
Publication Type: Journal Article
0022-2836
10.1016/0022-2836(75)90151-5 doi
Animals
Binding Sites
Cysteine--analysis
Disulfides--analysis
Dithiothreitol
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Pancreas
Protein Binding
Thermodynamics
Trypsin Inhibitors--analysis