Die Natur der Protein–Protein‐Wechselwirkung und ihr spektroskopischer Nachweis, dargestellt am Beispiel der Polyglycin–Insulin‐Aggregate

Weak intermolecular interactions between proteins may lead to mutual adaption of their secondary structures with the consequence of modified bioactivities. The basic possibilities of protein‐protein interactions are summarized in the light of their quantumchemically elucidated nature as well as their spectroscopic indications including modern mathematical tools for artficial resolution enhancement. In this way a clear differentiation between a mixture of proteins and their definite aggregates (complexes) becomes feasible. The example of insulin‐polyglycine mixtures and complexes is used to demonstrate scope and limitations of the FT‐IR spectroscopy in recognizing and interpreting protein‐protein interactions.