The monomeric, fast-acting hormone, mutant insulin B28 Pro --> Asp, has reduced the likely hood to form dimers and hexamers for therapeutic purposes. Around small phenolic derivatives mutant insulin B28 can create zinc hexamers, this is used as antimicrobial agents in insulin preparation. in the presence of phenol and m-cresol B28 Asp Insulin has been able to form crystals, containing aromatic side chains at the dimer-dimer interfaces and the monomer-monomer interfaces. However, at the monomer-monomer interfaces, there is a higher conformational flexibility in the B chains, caused by the B28 Pro --> Asp mutation. Additionally, this results in the loss of importance in the intermolecular force. It was discovered, that the binding of two m-cresol molecules disordered the beta- strand in a dimer. This indicated the cross link causes a strain on the B chain, which weakens the monomer-monomer interfaces.
Function
Disease
Relevance
Structural highlights
Alpha Helices,
Beta Strands ,
Loops ,
Turns.
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Additionally,
