Primary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility.

@article{Haas2009PrimarySO,
  title={Primary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility.},
  author={J{\"u}rgen Haas and Esteban V{\"o}hringer-Martinez and Andreas B{\"o}gehold and Dirk Matthes and Ulf Hensen and Avishay Pelah and Bernd Abel and Helmut Grubm{\"u}ller},
  journal={Chembiochem : a European journal of chemical biology},
  year={2009},
  volume={10 11},
  pages={1816-22}
}
Insulin aggregation critically depends on pH. The underlying energetic and structural determinants are, however, unknown. Here, we measure the kinetics of the primary aggregation steps of the insulin monomer in vitro and relate it to its conformational flexibility. To assess these primary steps the monomer concentration was monitored by mass spectrometry at various pH values and aggregation products were imaged by atomic force microscopy. Lowering the pH from 3 to 1.6 markedly accelerated the… CONTINUE READING

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