Cold denaturation of a protein dimer monitored at atomic resolution

Mariusz Jaremko, Łukasz Jaremko, Hai Young Kim, Min Kyu Cho, Charles D. Schwieters, Karin Giller, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)264-270
Number of pages7
JournalNature Chemical Biology
Issue number4
StatePublished - Apr 2013
Externally publishedYes

Bibliographical note

Funding Information:
We thank N. Rezaei-Ghaleh for useful discussions. This work was supported by the START and Ventures Programmes of Foundation for Polish Science (Fundacja na rzecz Nauki Polskiej; operated within the Innovative Economy Operational Programme (IE OP) 2007-2013 within European Regional Development Fund (L.J. and M.J.), the Iuventus Plus project no. IP2011 019471 from Polish Ministry of Sciences and Higher Education (M.J.) and the Cluster of Excellence and Deutsche Forschungsgemeinschaft Research Center “Nanoscale Microscopy and Molecular Physiology of the Brain” (to M.Z.). C.D.S. was supported by the Intramural Research Program of the Center for Information Technology at the US National Institutes of Health.

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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