Insulin hexamers: new conformations and applications.

@article{Brader1991InsulinHN,
  title={Insulin hexamers: new conformations and applications.},
  author={Mark Laurence Brader and Michael F. Dunn},
  journal={Trends in biochemical sciences},
  year={1991},
  volume={16 9},
  pages={
          341-5
        }
}
Recent studies on the structural and chemical properties of insulin have shown that the insulin hexamer is an allosteric protein capable of adopting three distinct conformations, designated T6, T3R3 and R6. Although the physiological consequences of this allostery are not established, new applications for the insulin hexamer as a model system for the study of allostery and for the study of zinc enzymes and copper proteins are emerging. 
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