Abstract
The dev analysis was used to construct the functional structure of protein (3). Based on this principle, the intramolecular interaction of dev peak was investigated. Two types of peak were observed: one is the hidden peak which interacts strongly with another region of the molecule and the other is the exposed peak whose interaction was weak. Analysis was made with trypsin and its inhibitor and on the intermolecular interaction between their exposed peaks. One interaction between their exposed peaks was found to coincide with one which had been already known to be authentic between their active sites.
