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...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 1980, Vol.346 (1), p.59-77
Main Authors: DeTraglia, Michael C., Brand, John S., Tometsko, Andrew M.
Format: Article
Language:English
Subjects:
Affinity Labels
Azides
Binding Sites
Hydrogen-Ion Concentration
Photochemistry
Photolysis
Protein Conformation
Proteins - metabolism
Trypsin Inhibitors
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Summary: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.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.1980.tb22091.x