Sandbox GGC2
From Proteopedia
(Difference between revisions)
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==Cross-Linked B28 ASP Insulin== | ==Cross-Linked B28 ASP Insulin== | ||
<StructureSection load='1ZEI' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1ZEI' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | The monomeric, fast-acting hormone, mutant insulin B28 Pro --> Asp, has reduced the likelyhood 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. | + | The monomeric, fast-acting hormone, mutant insulin B28 Pro --> Asp, has reduced the likelyhood 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 == | == Function == | ||
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== Relevance == | == Relevance == | ||
| + | B28 Asp Insulin is known to reduce dimers and hexamers for therapeutic purposes, which mainly include the ability to control blood glucose levels in the body. Additionally, this monomeric insulin is important in investigating the ability to aggregate in the presence of zinc and its effects on different structures in the molecule. | ||
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== Structural highlights == | == Structural highlights == | ||
Revision as of 14:05, 23 April 2018
Cross-Linked B28 ASP Insulin
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