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Cold denaturation of a protein dimer monitored at atomic resolution.

MPG-Autoren
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Jaremko,  M.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Jaremko,  L.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Kim,  H. Y.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Cho,  M. K.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Externe Ressourcen

http://www.nature.com/nchembio/journal/v9/n4/pdf/nchembio.1181.pdf
(Verlagsversion)

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1711711.pdf
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Zitation

Jaremko, M., Jaremko, L., Kim, H. Y., Cho, M. K., Schwieters, C. D., Giller, K., et al. (2013). Cold denaturation of a protein dimer monitored at atomic resolution. Nature Chemical Biology, 9(4), 264-270. doi:10.1038/nchembio.1181.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000E-ED7D-0
Zusammenfassung
Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 °C to −16 °C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding.