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Journal Article

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

MPS-Authors
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Haas,  J.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Vöhringer-Martinez,  E.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Matthes,  D.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Hensen,  U.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Pelah,  A.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Grubmuller,  H.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Fulltext (public)

1481738.pdf
(Publisher version), 677KB

Supplementary Material (public)

Haas_2009_cover-0.pdf
(Supplementary material), 327KB

Citation

Haas, J., Vöhringer-Martinez, E., Bögehold, A., Matthes, D., Hensen, U., Pelah, A., et al. (2009). Primary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility. ChemBioChem, 10(11), 1816-1822. doi:10.1002/cbic.200900266.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-A90E-2
Abstract
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