Application of light sensitive chemicals to probe protein structure and function.
These results suggest that important information regarding the conformation of complementary binding sites and the behavior of various charged states of inhibitors can be obtained from studies of the pH dependence of photoaffinity labeling experiments. This information may assist in identifying the pKas of key residues controlling the binding interaction. This technique should prove very useful in probing binding site structure on nonfunctioning targets, such as enzyme zymogens, as well as complicated receptor interactions.
D000345:Affinity Labels; D001386:Azides; D001665:Binding Sites; D006863:Hydrogen-Ion Concentration; D010777:Photochemistry; D010782:Photolysis; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D014361:Trypsin Inhibitors
D000345:Affinity Labels; D001386:Azides; D011506:Proteins; D014361:Trypsin Inhibitors