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  Cold denaturation of a protein dimer monitored at atomic resolution.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-ED7D-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-48B5-7
Genre: Journal Article

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 Creators:
Jaremko, M.1, Author              
Jaremko, L.1, Author              
Kim, H. Y.2, Author              
Cho, M. K.2, Author              
Schwieters, C. D., Author
Giller, K.1, Author              
Becker, S.1, Author              
Zweckstetter, M.2, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2013-02-102013-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nchembio.1181
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Title: Nature Chemical Biology
Source Genre: Journal
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Pages: - Volume / Issue: 9 (4) Sequence Number: - Start / End Page: 264 - 270 Identifier: -